Recombinant Human Minor histocompatibility antigen H13 (HM13), partial

Code CSB-YP851544HU
MSDS
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Source Yeast
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Code CSB-EP851544HU
MSDS
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Source E.coli
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Code CSB-EP851544HU-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-BP851544HU
MSDS
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Source Baculovirus
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Code CSB-MP851544HU
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
HM13
Uniprot No.
Alternative Names
dJ324O17.1; H13; hIMP1; Histocompatibility (minor) 13; HM13; HM13_HUMAN; IMP-1; IMP1; IMPAS; IMPAS-1; Intramembrane protease 1; Intramembrane protease; Minor histocompatibility antigen 13; Minor histocompatibility antigen H13; MSTP086; OTTHUMP00000030527; OTTHUMP00000030528; OTTHUMP00000030530; OTTHUMP00000214528; Presenilin-like protein 3; PSENL3; PSL3; Signal peptide peptidase; Signal peptide peptidase beta; SPP
Species
Homo sapiens (Human)
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, 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℃/-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.

Customer Reviews and Q&A

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Target Background

Function
Catalyzes intramembrane proteolysis of some signal peptides after they have been cleaved from a preprotein, resulting in the release of the fragment from the ER membrane into the cytoplasm. Required to generate lymphocyte cell surface (HLA-E) epitopes derived from MHC class I signal peptides. May be necessary for the removal of the signal peptide that remains attached to the hepatitis C virus core protein after the initial proteolytic processing of the polyprotein. Involved in the intramembrane cleavage of the integral membrane protein PSEN1. Cleaves the integral membrane protein XBP1 isoform 1 in a DERL1/RNF139-dependent manner. May play a role in graft rejection.
Gene References into Functions
  1. Preproinsulin signal peptide epitopes are processed by SPP and loaded for HLA-guided immune recognition via pathways that are enhanced during type 1 diabetes pathogenesis. PMID: 29343547
  2. Though far from complete, our knowledge on pathophysiological functions of SPP/SPPL proteases, in particular based on studies in mice, has been significantly increased over the last years. Based on this, inhibition of distinct SPP/SPPL proteases has been proposed as a novel therapeutic concept e.g. for the treatment of autoimmunity and viral or protozoal infections, as we will discuss in this review. PMID: 28624439
  3. The domains involved in HO-1 translocation have been identified, and it was shown that SPP-mediated HO-1 cleavage is isoform-specific (HO-1 vs HO-2) and independent of heme oxygenase activity. PMID: 29155886
  4. This study identifies that SPP affects EGFRvIII secretion profiles and thus promotes tumor progression, providing further understanding of the formation of secreted vesicles and driving role of EGFRvIII in Glioblastoma. PMID: 28198167
  5. structure of human SPP [SPP] PMID: 21636854
  6. identified human signal peptide peptidase as a polytopic membrane protein with sequence motifs characteristic of the presenilin-type aspartic proteases [SPP] PMID: 12077416
  7. identification and molecular cloning; expression analysis of the hIMP1 gene (located on chromosome 20) was performed in human cell tissues and transfected cell cultures [IMP1] PMID: 12139484
  8. widespread expression of SPP in many tissues PMID: 12972007
  9. signal peptide peptidase forms a homodimer that is labeled by an active site-directed gamma-secretase inhibitor PMID: 14704149
  10. IMP1 is a bi-aspartic polytopic protease capable of cleaving transmembrane proteins such as presenilin 2. PMID: 14741365
  11. The peptide structure corresponding to the C-terminal residues from H13 ribosomal protein was determined using magnetic resonance spectroscopy. PMID: 14988012
  12. data implicate SPP in the US2 pathway and indicate the possibility of a previously unknown function for this intramembrane-cleaving aspartic protease in dislocation from the endoplasmic reticulum PMID: 16738546
  13. Upon isolation of membranes and solubilization with detergent, the biochemical characteristics of SPP are remarkably similar to gamma-secretase. PMID: 16834339
  14. Compares a variant from the mouse ortholog to the human gene. PMID: 16730383

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Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein; Lumenal side.; [Isoform 4]: Cell membrane; Multi-pass membrane protein.
Protein Families
Peptidase A22B family
Tissue Specificity
Widely expressed with highest levels in kidney, liver, placenta, lung, leukocytes and small intestine and reduced expression in heart and skeletal muscle. Expressed abundantly in the CNS with highest levels in thalamus and medulla.
Database Links

HGNC: 16435

OMIM: 607106

KEGG: hsa:81502

UniGene: Hs.373741

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