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Biotinylated Hemofiltrate CC chemokine-1 (HCC-1/CCL14) 8021

$134.00$3,368.00

Summary

  • Expression: E.coli
  • Amino Acid Range: 28-93
SKU: 8021parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 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

protein
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
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

Migration Assay: Cells expressing recombinant CCR1 were assayed for migration through a transwell filter at various concentrations of WT or Biotinylated HCC-1. Responses are expressed as the % of total input cells (Blue: wild type; Red: biotinylated).
Migration Assay: Cells expressing recombinant CCR1 were assayed for migration through a transwell filter at various concentrations of WT or Biotinylated HCC-1. Responses are expressed as the % of total input cells (Blue: wild type; Red: biotinylated).

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.




pmidtitleauthorscitation

Protocols

relevant to this product
Migration assay

Documents

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