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Recombinant Human HTRA1 Mutant (L345G) Protein, Myc/DDK-tagged

Cat.No. : HTRA1-132H
Product Overview : Purified mutant recombinant protein of Human HtrA serine peptidase 1 (HTRA1), residues 161-369aa and mutation at(L345G) with a Myc/DDK tag was expressed in HEK293
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Description : This gene encodes a member of the trypsin family of serine proteases. This protein is a secreted enzyme that is proposed to regulate the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. It has also been suggested to be a regulator of cell growth. Variations in the promoter region of this gene are the cause of susceptibility to age-related macular degeneration type 7.
Source : HEK293
Species : Human
Tag : Myc/DDK
Molecular Mass : 22.5 kDa
Protein length : 161-369
Purity : > 80% as determined by SDS-PAGE and Coomassie blue staining
Stability : Stable for at least 12 months from receipt of products under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.
Storage : Store at -80 centigrade after receiving vials.
Concentration : > 50 μg/mL as determined by microplate Bradford method
Storage Buffer : 25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol
Gene Name : HTRA1 HtrA serine peptidase 1 [ Homo sapiens (human) ]
Official Symbol : HTRA1
Synonyms : HTRA1; HtrA serine peptidase 1; L56; HtrA; ARMD7; ORF480; PRSS11; CARASIL; CADASIL2; serine protease HTRA1; IGFBP5-protease
high-temperature requirement A serine peptidase 1; protease, serine, 11 (IGF binding); EC 3.4.21.-
Gene ID : 5654
mRNA Refseq : NM_002775
Protein Refseq : NP_002766
MIM : 602194
UniProt ID : Q92743

For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.

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Q&As (6)

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Is there a relationship between the structure and function of HTRA1 protein? 05/26/2023

The structure of the HTRA1 protein determines its function. The serine protease domain is the main functional region of HTRA1 protein, which has catalytic activity and can degrade proteins. In addition, the HTRA1 protein has a number of different domains that are closely related to its function.

Describe the treatment strategy of HTRA1 protein? 09/16/2022

Therapeutic strategies for HTRA1 protein include inhibiting its activity, regulating its expression level, and altering its structure. Several drugs are already undergoing clinical trials to evaluate their efficacy against cancer and other diseases.

How can disease be treated by regulating the expression of HTRA1 protein? 10/28/2021

There are currently no treatments that directly regulate HTRA1 protein expression. However, some diseases can be treated by inhibiting their activity or regulating their expression levels. For example, some drugs can inhibit the activity of the HTRA1 protein to treat cancer or Alzheimer's disease.

Is HTRA1 involved in cell signal transduction? 08/03/2021

HTRA1 protein can be used as a signal transduction molecule by binding to receptors on the cell surface to transmit signals to the cell interior and participate in cell proliferation, differentiation and apoptosis.

How does HTRA1 protein participate in extracellular matrix remodeling? 07/24/2021

This protein can degrade a variety of proteins in the extracellular matrix, including collagen, elastin and fibrin, and thus participate in extracellular matrix remodeling.

What method is used to detect the expression level of HTRA1 protein in biological samples? 06/15/2021

The expression level of HTRA1 protein in biological samples can be detected by immunohistochemistry, western blot and real-time quantitative PCR.

Customer Reviews (3)

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Reviews
06/06/2022

    The structure of HTRA1 is stable and not easy to mutate, which ensures the reliability of the experimental results.

    08/17/2021

      The solubility and ion exchange capacity are very good, which is convenient for subsequent experimental processing and purification.

      11/10/2020

        It is easy to operate and does not require complex operation steps.

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