h-1

Relaxin-1, also known as Prorelaxin H1 and RLN1, is a secreted protein that belongs to the insulin family. It is a peptide hormone that was first described in 1926 by Frederick Hisaw. Since its discovery as a reproductive hormone 8 years ago, relaxin has been implicated in a number of pregnancy-related functions involving extracellular matrix (ECM) turnover and collagen degradation. It is now becoming evident that relaxin's ability to reduce matrix synthesis and increase ECM degradation has important implications in several nonreproductive organs, including the heart, lung, kidney, liver and skin. The relaxin-like peptide family belongs in the insulin superfamily and consists of 7 peptides of high structural but low sequence similarity; relaxin-1 (RNL1), relaxin-2 (RNL2) and relaxin-3 ( RNL3), and the insulin-like (INSL) peptides, INSL3, INSL4, INSL5 and INSL6. The functions of relaxin-3, INSL4, INSL5, INSL6 remain uncharacterised. Relaxin-1 RLN1 is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. Relaxin-1 RLN1 may be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix. Relaxin and estrogen appear to play protective roles against airway fibrosis, airway SM thickening, and cardiac hypertrophy. Relaxin may also provide a means to regulate excessive collagen deposition during kidney development and in diseased states characterized by renal fibrosis.

Expression system: E. coli
Length: 26-614, Full Length of Mature Protein
Activity: Not Tested

Influenza A H3N2 (A Kansas 14 2017) (A Singapore INFIMH-16-0019 2016) Nucleoprotein NP Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 57.3 kDa.

Influenza A H3N2 (A Singapore INFIMH-16-0019 2016) Hemagglutinin HA Protein (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 59.27 kDa.

Tryptophan 5-hydroxylase 1, also known as Tryptophan 5-monooxygenase 1, Tryptophan hydroxylase 1, TPH1, TPH and TPRH, is an enzyme that belongs to the biopterin-dependent aromatic amino acid hydroxylase family. TPH1 contains one ACT domain. Tryptophan hydroxylase catalyzes the biopterin-dependent monooxygenation of tryptophan to 5-hydroxytryptophan (5HT), which is subsequently decarboxylated to form the neurotransmitter serotonin. It is the rate-limiting enzyme in the biosynthesis of serotonin. It is the rate-limiting enzyme in the biosynthesis of serotonin. TPH1 expression is limited to a few specialized tissues: raphe neurons, pinealocytes, mast cells, mononuclear leukocytes, beta-cells of the islets of Langerhans, and intestinal and pancreatic enterochromaffin cells. The tryptophan hydroxylase 1 (TPH1) gene is also reported to be associated with suicidal behavior. Polymorphisms of TPH1 may assist in identifying a subgroup of mood disorder patients that is at higher risk for suicidal behavior.

Influenza A H3N2 (A Singapore INFIMH-16-0019 2016) Neuraminidase NA Protein (His) is expressed in Baculovirus insect cells with His tag. The predicted molecular weight is 54.7 kDa.

Expression system: E. coli
Length: 2-253, Full Length of Mature Protein
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-239, Partial
Activity: ELISA

PD-L1 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-6xHis tag. The predicted molecular weight is 32-40 KDa and the accession number is G7PSE7.

Factor H is the major soluble inhibitor of complement, where its binding to self markers (i.e., particular glycan structures) prevents complement activation and amplification on host surfaces. Not surprisingly, mutations and polymorphisms that affect recognition of self by factor H are associated with diseases of complement dysregulation, such as age-related macular degeneration and atypical haemolytic uremic syndrome. In addition, pathogens (i.e., non-self) and cancer cells (i.e., altered-self) can hijack factor H to evade the immune response.

CFHR2 belongs to the complement factor H protein family. The human complement factor H protein family consists of the complement and immune regulators factor H, the factor H-like protein 1(FHL-1) and five factor H-related proteins (CFHR-1 to -5). Members of the H-related protein family are exclusively composed of individually folded protein domains, termed short consensus repeats (SCRs) or complement control modules. CFHR2 contains 4 Sushi (CCP SCR) domains and is expressed by the liver and secreted in plasma. CFHR2 might be involved in complement regulation. It can associate with lipoproteins and may play a role in lipid metabolism.

GMFB is a nerve growth factor which belongs to the actin-binding proteins ADF family, GMF subfamily. GMFB is involved in nervous system development, angiogenesis and immune function. It is especially crucial for the nervous system. GMFB causes brain cell differentiation, stimulates neural regeneration and inhibits tumor cell proliferation. It contains 1 ADF-H domain and is phosphorylated after phorbol ester stimulation. GMFB overexpression in astrocytes results in the increase of BDNF production. GMFB expression is increased by exercise, thus BDNF is important for exercise-induction of BDNF.

CFL1, also known as n-cofilin, is a member of the ADF Cofilin family. This family comprises three genes: CFL1, CFL2 and DSTN (destrin). ADF Cofilin family members bind G-actin monomers and depolymerize actin filaments through two mechanisms: severing and increasing the off-rate for actin monomers from the pointed end. Cofilin also binds with other proteins such as myosin, tropomyosin, α-actinin, gelsolin and scruin. These proteins compete with cofilin for actin binding. Сofilin also plays a role in innate immune response. CFL1 contains 1 ADF-H domain and is widely distributed in various tissues. It is important for normal progress through mitosis and normal cytokinesis.

Complement factor H CFH Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 43.8 kDa and the accession number is E9Q8I0.

Hemoglobin subunit alpha 1 (HBA1), also known as α2β2, is a hetero-tetramer consisting of two α and two β subunits held together by non-covalent interactions. Each subunit contains a heme group with an iron atom in the Fe2+ state. Cooperativity of Hemoglobin (Hb) in binding with O2 and allosteric regulatory binding properties with CO2, H+, Cl−, and 2,3-DPG (2,3-bisphosphoglycerate) are based on subunit interactions. HBA1 is the most common type of Hb in adult humans, which mediates the transport of oxygen and carbon dioxide in the blood. In recent years, Hb α and β chains have been found co-expressed in alveolar cells, mesangial cells of the kidney, retinal ganglion cells, hepatocytes and neurons. Endothelial and peripheral catecholaminergic cells express exclusively the α chain, while macrophages present the β chain only.

Expression system: HEK293 Cells
Length: 19-238, Partial
Activity: ELISA

Expression system: E. coli
Length: 1-321, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 45-646, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 1-643, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 57-642, Full Length of Mature Protein
Activity: Not Tested

Expression system: E. coli
Length: 22-305, Extracellular Domain
Activity: Not Tested

Expression system: E. coli
Length: 1-127, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-459, Full Length
Activity: Not Tested

Expression system: HEK293 Cells
Length: 1-178, Partial
Activity: Not Tested