Recombinant Mouse Myoglobin (Mb)

In Stock
Code CSB-MP013529MO
MSDS
Size $660
Order now
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

Have Questions? Leave a Message or Start an on-line Chat

Product Details

Purity
Greater than 85% as determined by SDS-PAGE.
Target Names
Mb
Uniprot No.
Research Area
Cancer
Alternative Names
Mb; Myoglobin
Species
Mus musculus (Mouse)
Source
Mammalian cell
Expression Region
2-154aa
Target Protein Sequence
GLSDGEWQLVLNVWGKVEADLAGHGQEVLIGLFKTHPETLDKFDKFKNLKSEEDMKGSEDLKKHGCTVLTALGTILKKKGQHAAEIQPLAQSHATKHKIPVKYLEFISEIIIEVLKKRHSGDFGADAQGAMSKALELFRNDIAAKYKELGFQG
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
21.9 kDa
Protein Length
Full Length of Mature Protein
Tag Info
N-terminal 10xHis-tagged and C-terminal Myc-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

The region for expressing recombinant Mouse Mb (Myoglobin) contains amino acids 2-154. This Mb (Myoglobin) protein is theoretically predicted to have a molecular weight of 21.9 kDa. This Mb (Myoglobin) recombinant protein is manufactured in mammalian cell. The N-terminal 10xHis tag and C-terminal Myc tag was fused into the coding gene segment of Mb (Myoglobin), making it easier to detect and purify the Mb (Myoglobin) recombinant protein in the later stages of expression and purification.

Mouse myoglobin (Mb) is a globular protein encoded by the Mb gene. Like its human counterpart, mouse myoglobin is primarily expressed in muscle tissues, where it plays a crucial role in oxygen storage and transport. Myoglobin is a heme-containing protein, with a single heme group per molecule that binds oxygen, allowing for its storage and release within muscle cells. This facilitates efficient oxygen supply to working muscles during periods of increased activity. Myoglobin is an essential component of the oxygen homeostasis machinery in muscle tissues. Research on mouse myoglobin helps to understand its role in oxygen metabolism, muscle function, and its implications in various physiological processes.

Customer Reviews and Q&A

 Customer Reviews

There are currently no reviews for this product.

Submit a Review here

Target Background

Function
Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles.
Gene References into Functions
  1. The authors here unravel a novel role of cardiac myoglobin in governing fatty acid metabolism to ensure the physiological energy production through beta-oxidation, preventing myocardial lipid accumulation and preserving cardiac functions. PMID: 28230173
  2. Inhibition of mammalian target of rapamycin (mTOR) activation using rapamycin restored Mb mRNA expression to control levels. Lipid supplementation had no effect on Mb gene expression. Thus, IGF-1-induced anabolic signaling can be a strategy to improve muscle size under mild hypoxia, but lowers Mb gene expression PMID: 28862673
  3. the novel cancer-associated MB splice variants exhibited increased expression in tumor cells subjected to experimental hypoxia; the novel gene regulatory mechanisms unveiled in this study support the idea of a non-canonical role of MB during carcinogenesis PMID: 24026678
  4. Myoglobin overexpression inhibits reperfusion in the ischemic mouse hindlimb through impaired angiogenesis but not arteriogenesis PMID: 24095922
  5. Chronic exercise downregulates myocardial myoglobin and attenuates nitrite reductase capacity during ischemia-reperfusion. PMID: 23962643
  6. Show a high capacity of myoglobin-deficient mice to adapt to catecholamine induced cardiac stress which is associated with activation of a distinct cardiac gene expression program. PMID: 20145201
  7. Endogenous nitrite reduction to NO. via the heme globin myoglobin enhances blood flow and matches O(2) supply to increased metabolic demands under hypoxic conditions. PMID: 22685116
  8. Myoglobin is present in the murine vasculature and contributes significantly to nitrite-induced vasodilation PMID: 20889759
  9. myoglobin constitutes the important barrier that efficiently protects the heart from nitrosative stress PMID: 12665503
  10. Findings demonstrate that myoglobin serves as an important cytoplasmic buffer of iNOS-derived NO, which determines the functional consequences of iNOS overexpression. PMID: 12775582
  11. myoglobin is an important cytoplasmic cardiac hemoprotein that functions in regulating NO homeostasis within cardiomyocytes. PMID: 12881221
  12. The role of myoglobin as intracellular nitric oxide(NO) scavenger is small, and increase in mitochondrial superoxide in SOD heterozygous mice may cause decrease NO bioavailability and alter control of myocardial O2 consumption by NO. PMID: 12919935
  13. analysis of amyloid-forming apomyoglobin mutant W7FW14F PMID: 14701846
  14. Mb is a key element influencing redox pathways in cardiac muscle to functionally and metabolically protect the heart from oxidative damage. PMID: 15132981
  15. importance of oxygen supply and nitric oxide scavenging by myoglobin is clearly demonstrated at the conscious animal level PMID: 15817640
  16. lack of myoglobin causes a biochemical shift in cardiac substrate utilization from fatty acid to glucose oxidation. PMID: 15817884
  17. In myoglobin-containing mouse heart endogenous chromophores interfere with Fura-2 fluorometry in myocardial ischemia. PMID: 17316820
  18. testosterone and training have differential effects on the concentration of myoglobin in some, but not all muscles PMID: 18548256
  19. myoglobin and the heme globin family subserve a critical function as an intrinsic nitrite reductase that regulates responses to cellular hypoxia and reoxygenation. PMID: 18632562
  20. Hypoxia reprograms calcium signaling and regulates myoglobin expression. PMID: 19005161

Show More

Hide All

Protein Families
Globin family
Database Links
CUSABIO guaranteed quality
icon of phone
Call us
301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
icon of address
Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
icon of social media
Join us with

Subscribe newsletter

Leave a message

* To protect against spam, please pass the CAPTCHA test below.
CAPTCHA verification
© 2007-2024 CUSABIO TECHNOLOGY LLC All rights reserved. 鄂ICP备15011166号-1
Place an order now

I. Product details

*
*
*
*

II. Contact details

*
*

III. Ship To

*
*
*
*
*
*
*

IV. Bill To

*
*
*
*
*
*
*
*