Recombinant Human REG1 protein (His tag)
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Recombinant Human REG1 protein (His tag) is a Human Full Length protein, in the 1 to 166 aa range, expressed in HEK 293 cells, with >97%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
PSPS, PSPS1, REG, REG1A, Lithostathine-1-alpha, Islet cells regeneration factor, Islet of Langerhans regenerating protein, Pancreatic stone protein, Pancreatic thread protein, Regenerating islet-derived protein 1-alpha, Regenerating protein I alpha, ICRF, PSP, PTP, REG-1-alpha
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human REG1 protein (His tag) (AB276375)
SDS-PAGE analysis of ab276375
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
REG1 interacts with numerous cellular processes including cell proliferation survival and differentiation. It is not part of a complex but it displays localization primarily in the pancreas influencing exocrine pancreatic secretion. It also appears in other tissues such as the small intestine. Important in tissue regeneration and protection REG1 helps in repairing damage especially in the context of injury or stress.
Pathways
REG1 influences cell growth and apoptosis regulation. It participates in pathways involving pancreatic acinar cell growth like those modulated by cytokines and inflammatory mediators. REG1 interacts with proteins such as REG3 and they both play essential roles in maintaining cellular homeostasis upon injury particularly in digestive organs.
Specifications
Form
Lyophilized
General info
Function
Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration.
Post-translational modifications
The composition of the O-linked carbohydrate on Thr-27 is complex and varied. In the crystallographic structure, the attached sugar appears to be N-acetylglucosamine, typical of an intracellular protein, rather than N-acetylgalactosamine.
Target data
Product promise
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