Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | P16627 |
express system | E.coli |
product tag | biotin at C-terminal |
purity | > 97% by SDS PAGE |
molecular weight | Predicted Molecular Mass: 10,219.5471 Da Extinction Coefficient: 19,300 M-1 cm-1 Actual Molecular Mass: 10,219.5471 Da by ESI Mass Spec |
available size | 10 µg, 100 µg, 2 µg, 50 µg |
endotoxin | <0.01 EU per 1μg of the protein by the LAL method |
Biotinylated Hemofiltrate CC chemokine-1 (HCC-1/CCL14) 8021
$134.00 – $3,368.00
Summary
- Expression: E.coli
- Amino Acid Range: 28-93
Biotinylated Hemofiltrate CC chemokine-1 (HCC-1/CCL14) 8021
protein |
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Database link: human P16627 |
Size and concentration 2, 10, 50, 100µg and lyophilized |
Form Lyophilized |
Storage Instructions Avoid repeated freeze-thaw cycles: • 12 months from date of receipt, -20 to -70 °C as supplied. • 1 month, 2 to 8 °C under sterile conditions after reconstitution. • 3 months, -20 to -70 °C under sterile conditions after reconstitution |
Storage buffer Reconstitution: Spin sample prior to reconstitution. Recommended concentration of 100µg/mL in sterile water. Shipping: Room Temp |
Purity > 97% by SDS PAGE and HPLC |
target relevance |
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Hemofiltrate CC chemokine-1(HCC-1/CCL14) is endogeneously expressed by numerous tissues. Upon processing of the N terminal residues of the full length HCC-1 by the uPA-plasmin system, the active form of HCC-1 is a strong agonist for CCR1, CCR5 and to a lesser extent CCR3, and causes chemotaxis of different types of leukocytes. The active form of HCC-1 is also shown as a potent inhibitor of HIV entry. |
Protein names Heat shock 70 kDa protein 1-like (Heat shock 70 kDa protein 1L) (Heat shock 70 kDa-like protein 1) (Spermatid-specific heat shock protein 70) |
Gene names Hspa1l,Hspa1l Hsc70t |
Protein family Heat shock protein 70 family |
Mass 70637Da |
Function Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. Positive regulator of PRKN translocation to damaged mitochondria. |
Tissues Expressed in spermatids. |
Structure Interacts with PRKN. |
Domain The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsi |
Target Relevance information above includes information from UniProt accession: P16627 |
The UniProt Consortium |
Data
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.pmid | title | authors | citation |
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Protocols
relevant to this product |
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Migration assay |
Documents
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