Recombinant Chicken Spectrin alpha chain, brain (SPTAN1), partial

Code CSB-YP022633CH
MSDS
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Source Yeast
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Code CSB-EP022633CH
MSDS
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Source E.coli
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Code CSB-EP022633CH-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP022633CH
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP022633CH
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
SPTAN1; SPTA2Spectrin alpha chain; non-erythrocytic 1; Alpha-II spectrin; Fodrin alpha chain
Species
Gallus gallus (Chicken)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
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 before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
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℃/-80℃. 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
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Morphologically, spectrin-like proteins appear to be related to spectrin, showing a flexible rod-like structure. They can bind actin but seem to differ in their calmodulin-binding activity. In nonerythroid tissues, spectrins, in association with some other proteins, may play an important role in membrane organization.
Gene References into Functions
  1. Tracking of the NMR HN peak intensities for 2 weeks reports on site-specific hydrogen bond strength and also likely reflects water accessibility in a qualitative manner. PMID: 28393279
  2. Spectroscopic study of the thermal stability of chicken brain alpha-spectrin repeat 17. PMID: 22569754
  3. kinetic characterisation of the wild-type forms of the 15th, 16th, and 17th domains of brain alpha-spectrin PMID: 15504411
  4. protein engineering phi-value analysis of the 16th domain of brain alpha-spectrin PMID: 15504412
  5. Data show that mutation of alpha-spectrin asparagine 47 to alanine induces the formation of amyloid fibrils under mild acid conditions. PMID: 16375922
  6. Results describe the folding pathway of the 17th domain of chicken brain alpha-spectrin, R17. PMID: 16618492
  7. The high-resolution structure of the complex between the R21A mutant of Spc-SH3 and p41 derived from nuclear magnetic resonance data, is presented. PMID: 17407569
  8. Spectrin-titin domain pairs of both spectrin R16 and R17 with a single titin I27 domain at either the N- or the C-terminus were created and found that spectrin domains are significantly stabilized, by nonnative interactions at the C-terminus only. PMID: 17890397
  9. The rate-limiting transition state for R15 folding is investigated using protein engineering methods (Phi-value analysis) and compared with previously completed analyses of R16 and R17 (15th, 16th repeats of alpha-spectrin). PMID: 19445951

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Subcellular Location
Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
Protein Families
Spectrin family
Database Links
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301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
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7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
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