Search: 1000 results found for "Glucagon"

Description:

GrpE-Like 1 Human Recombinant

HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.

Product # :

PRO-263

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Description

GRPEL1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 211 amino acids (28-217a.a.) and having a molecular mass of 23.6kDa.GRPEL1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GRPEL1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
GRPEL1 is a vital component of the PAM complex, a complex necessary for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. GRPEL1 protein controls the nucleotide-dependent binding of mitochondrial HSP70 to substrate proteins.
Synonyms
HMGE, GrpE-like protein cochaperone, GREPEL1, FLJ25609.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MCTATKQKNS GQNLEEDMGQ SEQKADPPAT EKTLLEEKVK LEEQLKETVE KYKRALADTE NLRQRSQKLV EEAKLYGIQA FCKDLLEVAD VLEKATQCVP KEEIKDDNPH LKNLYEGLVM TEVQIQKVFT KHGLLKLNPV GAKFDPYEHE ALFHTPVEGK EPGTVALVSK VGYKLHGRTL RPALVGVVKE A

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

DiGeorge Syndrome Critical Region Gene 6 Human Recombinant

DiGeorge syndrome critical region gene 6, Protein DGCR6, DGCR6.

Product # :

PRO-1372

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Description

DGCR6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27kDa. DGCR6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

DGCR6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
DiGeorge syndrome critical region gene 6 (DGCR6) shares homology with the Drosophila melanogaster gonadal protein, that participates in gonadal and germ cell development, and also with the gamma-1 subunit of human laminin. DGCR6 is involved in DiGeorge syndrome pathology and in schizophrenia.
Synonyms
DiGeorge syndrome critical region gene 6, Protein DGCR6, DGCR6.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMERYAGA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVLQA AQQRELEAVE HRIREEQRAM DQKIVLELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCWAGKAA LGLGGPWQLP AAQCDQKGSP VPP.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Epigen Human Recombinant, His Tag

EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.

Product # :

CYT-794

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Description

EPGN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 111 amino acids (23-110 a.a) and having a molecular mass of 12.1kDa.EPGN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EPGN protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
EPGN is an EGF-related polypeptide growth factor that signals through the ErbB receptor-1. EPGN is produced in numerous tissues, including the testis, liver, heart and in certain tumor cells. EPGN is mitogenic for fibroblasts and epithelial cells. Human EPGN is originally synthesized as a glycosylated 14.7 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a mature soluble sequence.
Synonyms
EPG, Epigen, PRO9904, ALGV3072, FLJ75542, EPGN, Epithelial mitogen.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K
Background
What is the molecular weight/Mw of EPIGEN Protein?
EPIGEN Protein has a total Mw of 12.1kDa.

What is the source or expression system of EPIGEN Protein?
Escherichia Coli.

What is the Purity of EPIGEN Protein?
EPIGEN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of EPIGEN Protein?
The biological functionality of EPIGEN Protein will be determined in the future.

What is the amino acid sequence of EPIGEN Protein?
MGSSHHHHHH SSGLVPRGSH MGSAAVTVTP PITAQQGNWT VNKTEADNIE GPIALKFSHL CLEDHNSYCI NGACAFHHEL EKAICRCFTG YTGERCEHLT LTSYAVDSYE K

What applications can EPIGEN Protein be used in?
EPIGEN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EPIGEN Protein?
The endotoxin level is minimal, EPIGEN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

F-Box Protein 6 Human Recombinant

FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.

Product # :

PRO-1522

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Description

FBXO6 Human Recombinant produced in E. coli is a single polypeptide chain containing 316 amino acids (1-293) and having a molecular mass of 36.3kDa. FBXO6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The FBXO6 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
F-Box Protein 6, also known as FBXO6, is a part of the F-box protein family which is characterized by a roughly forty amino acid motif, the F-box. The F-box proteins are one of the 4 subunits of the ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box) that operates in phosphorylation-dependent ubiquitination. The F-box proteins are divided into three categories: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing different protein-protein interaction modules or no recognizable motifs. FBXO6 is a part of the Fbxs category, and its C-terminal area is very similar to that of rat NFB42 (neural F Box 42 kDa) which is involved in the control of the cell cycle.
Synonyms
FBG2, FBS2, FBX6, Fbx6b, F-box only protein 6, F-box protein that recognizes sugar chains 2, F-box/G-domain protein 2, FBXO6.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDAPHSK AALDSINELP ENILLELFTH VPARQLLLNC RLVCSLWRDL IDLMTLWKRK CLREGFITKD WDQPVADWKI FYFLRSLHRN LLRNPCAEED MFAWQIDFNG GDRWKVESLP GAHGTDFPDP KVKKYFVTSY EMCLKSQLVD LVAEGYWEEL
LDTFRPDIVV KDWFAARADC GCTYQLKVQL ASADYFVLAS FEPPPVTIQQ WNNATWTEVS YTFSDYPRGV RYILFQHGGR DTQYWAGWYG PRVTNSSIVV SPKMTRNQAS SEAQPGQKHG QEEAAQSPYR AVVQIF.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Fibrinogen Beta Chain Human Recombinant

Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.

Product # :

PRO-2210

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Description

FGB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 351 amino acids (164-491a.a) and having a molecular mass of 40kDa. FGB is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FGB protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Fibrinogen Beta Chain 9 (FGB) is the beta component of fibrinogen, a blood-borne glycoprotein composed of 3 pairs of nonidentical polypeptide chains. When vascular injury accrues, fibrinogen is cleaved by thrombin to form fibrin which is found in abundance in blood clots.
Synonyms
Fibrinogen beta chain, Fibrinopeptide B, Fibrinogen, B Beta Polypeptide, Epididymis Secretory Sperm Binding Protein Li 78p, HEL-S-78p.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDNENVVN EYSSELEKHQ LYIDETVNSN IPTNLRVLRS ILENLRSKIQ KLESDVSAQM EYCRTPCTVS CNIPVVSGKE CEEIIRKGGE TSEMYLIQPD SSVKPYRVYC DMNTENGGWT VIQNRQDGSV DFGRKWDPYK QGFGNVATNT DGKNYCGLPG EYWLGNDKIS QLTRMGPTEL LIEMEDWKGD KVKAHYGGFT VQNEANKYQI SVNKYRGTAG NALMDGASQL MGENRTMTIH NGMFFSTYDR DNDGWLTSDP RKQCSKEDGG GWWYNRCHAA NPNGRYYWGG QYTWDMAKHG TDDGVVWMNW KGSWYSMRKM SMKIRPFFPQ Q.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Calcyclin Binding Protein Human Recombinant

S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.

Product # :

PRO-831

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Description

CACYBP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids (1-185a.a.) and having a molecular mass of 23.4 kDa. CACYBP protein is fused to a 20 amino acid His tag at N-terminus and is purified by standard chromatography.

Source

Escherichia Coli.

Formulation

CACYBP Human solution containing 20mM Tris HCL pH-8, 1mM DTT, 0.1M NaCl & 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
CACYBP (calcyclin binding protein) participates in calcium-dependent ubiquitination and subsequent proteosomal degradation of target proteins. CACYBP acts as a molecular bridge in ubiquitin E3 complexes. CACYBP is involved in the ubiquitin-mediated degradation of beta-catenin.
Synonyms
S100A6BP, S100A6 Binding Protein, GIG5, PNAS-107, RP1-102G20.6, SIP, CACYBP, hCacyBP, Siah-interacting protein, MGC87971.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQQKSQKKAE LLDNEKPAAV VAPITTGYTV KISNYGWDQS DKFVKIYITL TGVHQVPTEN VQVHFTERSF DLLVKNLNGK SYSMIVNNLL KPISVEGSSK KVKTDTVLIL CRKKVENTRW DYLTQVEKEC KEKEKPSYDT ETDPSEGLMN VLKKIYEDGD DDMKRTINKA WVESREKQAK GDTEF.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Calcium Modulating Ligand Human Recombinant

Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.

Product # :

PRO-1612

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Description

CAMLG Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189) and having a molecular mass of 23.2kDa.CAMLG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The CAMLG solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
CAMLG binds to cyclophilin B and operates downstream of the TCR and upstream of calcineurin by causing an influx of calcium. CAMLG is an essential membrane protein that takes part in the calcium signal transduction pathway, connecting cyclophilin B to calcium signaling.
Synonyms
Calcium Modulating Ligand, Calcium-Modulating Cyclophilin Ligand, Calcium-Signal Modulating Cyclophilin Ligand, Cyclophilin B-Binding Protein, CAML.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMESMAVA TDGGERPGVP AGSGLSASQR RAELRRRKLL MNSEQRINRI MGFHRPGSGA EEESQTKSKQ QDSDKLNSLS VPSVSKRVVL GDSVSTGTTD QQGGVAEVKG TQLGDKLDSF IKPPECSSDV NLELRQRNRG DLTADSVQRG SRHGLEQYLS RFEEAMKLRK QLISEKPSQE DGNTTEEFDS FR

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Germinal Center-Associated, Signaling and Motility Human Recombinant

GCAT2, HGAL, Germinal center-associated signaling and motility protein, Germinal center B-cell-expressed transcript 2 protein, Germinal center-associated lymphoma protein, GAL, GCET2 .

Product # :

PRO-1282

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Description

GCSAM Human Recombinant produced in E. coli is a single polypeptide chain containing 201 amino acids (1-178) and having a molecular mass of 23 kDa. GCSAM is fused to 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The GCSAM solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol and 1mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
GCSAM is a protein which functions in signal transduction pathways and whose expression raises in germinal cell lymphomas. GCSAM contains a putative PDZ-interacting domain, an immunoreceptor tyrosine-based activation motif (ITAM), and two putative SH2 binding sites. In B cells, GCSAM expression is particularly induced by interleukin-4.
Synonyms
GCAT2, HGAL, Germinal center-associated signaling and motility protein, Germinal center B-cell-expressed transcript 2 protein, Germinal center-associated lymphoma protein, GAL, GCET2 .
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMGNSLLR ENRRQQNTQE MPWNVRMQSP KQRTSRCWDH HIAEGCFCLP WKKILIFEKR QDSQNENERM SSTPIQDNVD QTYSEELCYT LINHRVLCTR PSGNSAEEYY ENVPCKAERP RESLGGTETE YSLLHMPSTD PRHARSPEDE YELLMPHRIS SHFLQQPRPL MAPSETQFSH L.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glucose-6-Phosphate Isomerase Human Recombinant

Glucose-6-phosphate isomerase, Phosphoglucose isomerase, Phosphohexose isomerase, Autocrine motility factor, Neuroleukin, Sperm antigen 36, GPI, PGI, PHI, AMF, NLK, SA-36, GNPI.

Product # :

ENZ-430

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Description

GPI Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 578 amino acids (1-558 a.a.) and having a molecular mass of 65.3kDa.The GPI is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GPI solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Glucose-6-phosphate isomerase (GPI) is a part of the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. GPI is a dimeric enzyme which catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Mammalian GPI also functions as a tumor-secreted cytokine and an angiogenic factor (AMF) which stimulates endothelial cell motility. In addition, GPI is a neurotrophic factor (Neuroleukin) for spinal and sensory neurons. GPI performs in different capacities inside and outside the cell. In the cytoplasm, GPI is involved in glycolysis and gluconeogenesis, while outside the cell it acts as a neurotrophic factor for spinal and sensory neurons.
Defects in the GPI gene cause the nonspherocytic hemolytic anemia and a severe enzyme deficiency can be linked to hydrops fetalis, immediate neonatal death and neurological impairment.
Synonyms
Glucose-6-phosphate isomerase, Phosphoglucose isomerase, Phosphohexose isomerase, Autocrine motility factor, Neuroleukin, Sperm antigen 36, GPI, PGI, PHI, AMF, NLK, SA-36, GNPI.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAALTRDPQF QKLQQWYREH RSELNLRRLF DANKDRFNHF SLTLNTNHGH ILVDYSKNLV TEDVMRMLVD LAKSRGVEAA RERMFNGEKI NYTEGRAVLH VALRNRSNTP ILVDGKDVMP EVNKVLDKMK SFCQRVRSGD WKGYTGKTIT DVINIGIGGS DLGPLMVTEA LKPYSSGGPR VWYVSNIDGT HIAKTLAQLN PESSLFIIAS KTFTTQETIT NAETAKEWFL QAAKDPSAVA KHFVALSTNT TKVKEFGIDP QNMFEFWDWV GGRYSLWSAI GLSIALHVGF DNFEQLLSGA HWMDQHFRTT PLEKNAPVLL ALLGIWYINC FGCETHAMLP YDQYLHRFAA YFQQGDMESN GKYITKSGTR VDHQTGPIVW GEPGTNGQHA FYQLIHQGTK MIPCDFLIPV QTQHPIRKGL HHKILLANFL AQTEALMRGK STEEARKELQ AAGKSPEDLE RLLPHKVFEG NRPTNSIVFT KLTPFMLGAL VAMYEHKIFV QGIIWDINSF DQWGVELGKQ LAKKIEPELD GSAQVTSHDA STNGLINFIK QQREARVQ.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Regulator of G-Protein Signaling 17 Human Recombinant

Regulator of G-protein signaling 17, RGS-17, RGSZ2, hRGS17.

Product # :

PRO-924

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Description

RGS17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (1-210) and having a molecular mass of 26.5 kDa.The RGS17 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The RGS17 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl,1mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
RGS17 weakens the signaling activity of G-proteins by binding to activated GTP-bound G alpha subunits and performing as a GTPase activating protein (GAP), increasing the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, creating inactive G-protein heterotrimers, which terminates the signal. RGS17 has a vital part in ending the signaling by mu opioid receptors and development of tolerance to opioid analgesic drugs.
Synonyms
Regulator of G-protein signaling 17, RGS-17, RGSZ2, hRGS17.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MRKRQQSQNE GTPAVSQAPG NQRPNNTCCF CWCCCCSCSC LTVRNEERGE NAGRPTHTTK MESIQVLEEC QNPTAEEVLS WSQNFDKMMK APAGRNLFRE FLRTEYSEEN LLFWLACEDL KKEQNKKVIE EKARMIYEDY ISILSPKEVS LDSRVREVIN RNLLDPNPHM YEDAQLQIYT LMHRDSFPRF LNSQIYKSFV ESTAGSSSES.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Thymulin

Product # :

HOR-047

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Thymulin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 858 Dalton and a Molecular formula of C33H54N12O15.

Formulation

The protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by RP-HPLC.

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thymulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymulin should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Thymulin in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.
Background
Thymulin, a nonapeptide hormone, is produced primarily by the thymus gland and has been recognized for its pivotal role in the immune system. It plays a significant role in the maturation and differentiation of T lymphocytes, which are crucial for immune function. Beyond its immune-related functions, research has increasingly unveiled the diverse physiological roles of thymulin. This study aims to comprehensively investigate thymulin, shedding light on its immunological functions and exploring its potential applications in various aspects of health and medicine.
The primary objective of this research is to elucidate the mechanisms underlying thymulin's role in immune regulation. In vitro and in vivo experiments will be conducted to explore thymulin's interactions with immune cells, its impact on T cell development and function, and its potential modulation of immune responses. Understanding these mechanisms is fundamental for harnessing thymulin's immunomodulatory properties.
The second objective is to assess the clinical relevance of thymulin in immune-related disorders. Clinical trials and studies involving individuals with autoimmune diseases, immunodeficiencies, and age-related immune decline will be conducted to evaluate the potential therapeutic applications of thymulin. These investigations may offer insights into the use of thymulin as an immunomodulatory agent in various clinical settings.
The third objective is to explore the broader implications of thymulin in health and medicine. Research will investigate its potential roles in areas beyond immunology, such as neuroprotection, wound healing, and tissue regeneration. Understanding the multifaceted properties of thymulin may open new avenues for therapeutic interventions in various medical specialties.
By delving into the diverse functions of thymulin, this research aims to expand our knowledge of its physiological roles and clinical applications. The findings may have implications for the development of innovative approaches in immunology and healthcare, ultimately benefiting patients affected by immune-related disorders and other medical conditions.
What is the molecular weight/Mw of THYMALIN Protein?
THYMALIN Protein has a total Mw of 0.85kDa.

What is the Purity of THYMALIN Protein?
THYMALIN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of THYMALIN Protein?
The biological functionality of THYMALIN Protein will be determined in the future.

What is the amino acid sequence of THYMALIN Protein?
Pyr-Ala-Lys-Ser-Gln-Gly-Gly-Ser-Asn-OH.

What applications can THYMALIN Protein be used in?
THYMALIN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for THYMALIN Protein?
The endotoxin level is minimal, THYMALIN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Carcinoembryonic Antigen-Related Cell Adhesion Molecule 7 Human Recombinant

CEA, CGM2, Carcinoembryonic antigen CGM2.

Product # :

PRO-1483

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Description

CEACAM7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (36-242 a.a.) and having a molecular mass of 25.7kDa.CEACAM7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CEACAM7 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Carcinoembryonic Antigen-Related Cell Adhesion Molecule 7 (CEACAM7) is a member of the immunoglobulin superfamily, CEA family. CEACAM7 contains 1 Ig-like C2-type (immunoglobulin-like) domain and 1 Ig-like V-type (immunoglobulin-like) domain. CEACAM7 is intensely down-regulated in colonic adenocarcinomas.
Synonyms
CEA, CGM2, Carcinoembryonic antigen CGM2.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSTNIDVVP FNVAEGKEVL LVVHNESQNL YGYNWYKGER VHANYRIIGY VKNISQENAP GPAHNGRETI YPNGTLLIQN VTHNDAGIYT LHVIKENLVN EEVTRQFYVF SEPPKPSITS NNFNPVENKD IVVLTCQPET QNTTYLWWVN NQSLLVSPRL LLSTDNRTLV LLSATKNDIG PYECEIQNPV GASRSDPVTL NVRYESVQAS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Hydroxyacylglutathione Hydrolase Human Recombinant

GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.

Product # :

ENZ-034

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Description

HAGH produced in E.Coli is a single, non-glycosylated polypeptide chain containing 284 amino acids (1-260a.a.) and having a molecular mass of 31.4kDa.HAGH is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HAGH protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl Buffer (pH 8.5) and 10% Glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
HAGH is a part of the glyoxalase family and a thiolesterase which hydrolyses S-lactoyl-glutathione to reduced glutathione and D-lactate. HAGH protein is a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73 and serves as a pro-survival factor of the p53 family. HAGH appears only as a monomer and binds two zinc ions per subunit.
Synonyms
GLX2, Glyoxalase II, GLO2, Hydroxyacyl Glutathione Hydrolase, HAGH1, GLXII, Hydroxyacylglutathione Hydrolase, hydroxyacylglutathione hydroxylase.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMKVEVL PALTDNYMYL VIDDETKEAA IVDPVQPQKV VDAARKHGVK LTTVLTTHHH WDHAGGNEKL VKLESGLKVY GGDDRIGALT HKITHLSTLQ VGSLNVKCLA TPCHTSGHIC YFVSKPGGSE PPAVFTGDTL FVAGCGKFYE GTADEMCKAL LEVLGRLPPD TRVYCGHEYT INNLKFARHV EPGNAAIREK LAWAKEKYSI GEPTVPSTLA EEFTYNPFMR VREKTVQQHA GETDPVTTMR AVRREKDQFK MPRD.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Corticotropin Releasing Hormone Binding Protein Human Recombinant

Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.

Product # :

HOR-267

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Description

CRHBP Human Recombinant is a 34.58 kDa protein containing 308 aa and fused to a 10 aa N-Terminal His-tag. CRHBP is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CRHBP Human was filtered (0.4µm) and lyophilized from 0.5mg/ml supplied in 20mM TRIS and 20mM NaCl, pH 7.5.

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Introduction
CRH is a powerful stimulator of synthesis and secretion of preopiomelanocortin-derived peptides. CRH concentration in the human peripheral circulation is usually low. The concentration rises during pregnancy and fall back quickly after parturition. Maternal plasma CRH most likely originates from the placenta. Human plasma has a CRH-binding protein that inactivates CRH and can inhibit inappropriate pituitary-adrenal stimulation in pregnancy.
Synonyms
Corticotropin releasing hormone binding protein, CRF-BP, CRH-BP, CRF-binding protein.
Physical Appearance
Filtered white lyophilized powder.
Stability
Store lyophilized protein at -20°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80°C for long term storage. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
Solubility
Add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
MKHHHHHHAS YLELREAADY DPFLLFSANL KRELAGEQPY RRALRCLDML SLQGQFTFTA DRPQLHCAAF FISEPEEFIT IHYDQVSIDC QGGDFLKVFD GWILKGEKFP SSQDHPLPSA ERYIDFCESG LSRRSIRSSQ NVAMIFFRVH EPGNGFTLTI KTDPNLFPCN VISQTPNGKF TLVVPHQHRN CSFSIIYPVV IKISDLTLGH VNGLQLKKSS AGCEGIGDFV ELLGGTGLDP SKMTPLADLC YPFHGPAQMK VGCDNTVVRM VSSGKHVNRV TFEYRQLEPY ELENPNGNSI GEFCLSGL YLELREAADY DPFLLFSANL KRELAGEQPY RRALRCLDML SLQGQFTFTA DRPQLHCAAF FISEPEEFIT IHYDQVSIDC QGGDFLKVFD GWILKGEKFP SSQDHPLPSA ERYIDFCESG LSRRSIRSSQ NVAMIFFRVH EPGNGFTLTI KTDPNLFPCN VISQTPNGKF TLVVPHQHRN CSFSIIYPVV IKISDLTLGH VNGLQLKKSS AGCEGIGDFV ELLGGTGLDP SKMTPLADLC YPFHGPAQMK VGCDNTVVRM VSSGKHVNRV TFEYRQLEPY ELENPNGNSI GEFCLSGL
Applications
ELISA, Western blotting

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Leptin Chicken Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-505

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Description

Leptin Chicken Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 145 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.

Purity

Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its activity is however 5-10 fold lower as compared to mammalian leptins.

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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Cys-Gln.
Recombinant Chicken leptin was produced according to the a.a. sequence published by the groups of Taouis & McMutry, see Raver et al. Protein Expr Purif. 1998 Dec; 14(3):403-8.
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.19 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC,using calibrated solution of Leptin Chicken as a Reference Standard.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Leptin Rabbit Recombinant

OB Protein, Obesity Protein, OBS, Obesity factor.

Product # :

CYT-507

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Description

Leptin Rabbit Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

Purity

Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.

More Info

Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 0.4% NaHCO3 adjusted to pH-8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.505 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Interferon-Omega 1 Human Recombinant, HEK

IFN omega-1, IFN alpha-II-1, IFNW1.

Product # :

CYT-1225

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Description

IFNW1 Human Recombinant is a single, glycosylated, polypeptide chain (22-195 a.a) containing a total of 180 amino acids and having a molecular mass of 20.9 kDa. IFNW1 is fused to a 6 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

The IFNW1 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .

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Synonyms
IFN omega-1, IFN alpha-II-1, IFNW1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.
Background
Interferons, a family of signaling proteins, play a pivotal role in the immune system’s defense against viral infections and other threats. Among these, Interferon W1 (IFNW1), a member of the Type I interferon family, has emerged as a key player in orchestrating antiviral responses and modulating immune reactions. This research embarks on a detailed exploration of the IFNW1 protein, unveiling its structural intricacies, signaling pathways, and its broader implications in immune regulation and disease. By delving into IFNW1, scientists aim to comprehend the nuances of its functions, decipher its interactions within the complex interferon network, and explore its potential applications in therapeutic interventions and beyond.
Structural Insights into IFNW1:
IFNW1, like other Type I interferons, exhibits a unique tertiary structure that enables it to interact with specific cell surface receptors. This interaction triggers a cascade of events, leading to the activation of various antiviral genes and immune modulatory pathways. Understanding the structural basis of IFNW1 is crucial for elucidating its binding affinities, biological activities, and its significance in immune responses.
Signaling Pathways and Antiviral Defense:
IFNW1 engages with its cognate receptors, initiating Janus kinase (JAK)-Signal Transducer and Activator of Transcription (STAT) signaling pathways. This activation leads to the transcription of interferon-stimulated genes (ISGs) with potent antiviral properties. IFNW1’s ability to induce an antiviral state in infected and neighboring cells is fundamental for restricting viral replication and curtailing the spread of infections. Additionally, IFNW1 plays a role in modulating adaptive immune responses, contributing to the broader immune defense mechanisms.
IFNW1 in Immunomodulation and Disease:
Beyond its antiviral functions, IFNW1 is implicated in immunomodulation and disease pathogenesis. Dysregulation of IFNW1 signaling is associated with autoimmune disorders, including lupus and rheumatoid arthritis, highlighting its involvement in immune-related diseases. Moreover, IFNW1 is being explored in cancer immunotherapy, where its ability to modulate the tumor microenvironment and enhance immune surveillance presents opportunities for novel treatment strategies.
Therapeutic Potential and Future Prospects:
The unique properties of IFNW1, particularly its role in immune regulation and antiviral defense, position it as a potential therapeutic target. Research efforts are directed towards harnessing its immunomodulatory functions for developing therapies against infectious diseases, autoimmune disorders, and certain cancers. Additionally, understanding IFNW1’s interactions with other components of the immune system opens avenues for innovative approaches in personalized medicine and targeted immunotherapies.
IFNW1 Protein, as an integral component of the interferon network, stands as a sentinel in the body’s defense against viral invasions and immune dysregulations. Its multifaceted roles in antiviral defense, immune modulation, and disease pathogenesis underscore its significance in biology and medicine. As researchers delve deeper into the intricacies of IFNW1, they pave the way for innovative therapies, immunomodulatory interventions, and a deeper understanding of immune responses. This research not only illuminates the pivotal role of IFNW1 but also holds the promise of transformative advancements in medicine, shaping the future of immunology and disease therapeutics.
What is the molecular weight/Mw of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein has a total Mw of 20.9kDa.

What is the source or expression system of IFNW1 HUMAN, HEK Protein?
HEK293 Cells.

What is the Purity of IFNW1 HUMAN, HEK Protein?
IFNW1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of IFNW1 HUMAN, HEK Protein?
The ED50 is ≤0.07 ng/ml, measured in a cytotoxicity assay using TF-1 human erythroleukemic cells .

What is the amino acid sequence of IFNW1 HUMAN, HEK Protein?
LGCDLPQNHG LLSRNTLVLL HQMRRISPFL CLKDRRDFRF PQEMVKGSQL QKAHVMSVLH EMLQQIFSLF HTERSSAAWN MTLLDQLHTG LHQQLQHLET CLLQVVGEGE SAGAISSPAL TLRRYFQGIR VYLKEKKYSD CAWEVVRMEI MKSLFLSTNM QERLRSKDRD LGSSHHHHHH.

What applications can IFNW1 HUMAN, HEK Protein be used in?
IFNW1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFNW1 HUMAN, HEK Protein?
The endotoxin level is minimal, IFNW1 HUMAN, HEK Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Galactosidase-Beta 1 E.coli Recombinant

lacZ, beta-gal, β-gal.

Product # :

ENZ-041

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Description

The E.Coli derived recombinant protein Beta-galactosidase (114 kDa) is enzymatically inactive and Non-reactive with human serum.

Source

Escherichia Coli.

Formulation

Beta-Galactosidase (1mg/1ml) is formulated in 8M urea, 20mM Tris-HCl pH 8.0, and 10mM beta-mercaptoethanol

Purity

Protein is >95% pure as determined by SDS-PAGE, by measuring optical density at 280 nm and by method of Bradford et al.

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Introduction
Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.
Synonyms
lacZ, beta-gal, β-gal.
Physical Appearance
Sterile filtered colorless solution.
Stability
Protein should be stored for Short Term at 4°C and for long term at -20°C.
Purification Method
Purified by proprietary chromatographic technique.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Meteorin Mouse Recombinant

Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.

Product # :

PRO-2241

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Description

METRN produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 276 amino acids (22-291 a.a.) and having a molecular mass of 30.2kDa (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). METRN is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

METRN protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Meteorin (METRN) is involved in both glial cell differentiation and axonal network formation during neurogenesis. METRN promotes astrocyte differentiation and transforms cerebellar astrocytes into radial glia. Moreover, the METRN protein stimulates axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
Synonyms
Meteorin, Hypoxia/reoxygenation regulatory factor, Metrn, 1810034B16Rik, Hyrac.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
GYSEDRCSWR GSGLTQEPGS VGQLTLDCTE GAIEWLYPAG ALRLTLGGPD PGTRPSIVCL RPERPFAGAQ VFAERMTGNL ELLLAEGPDL AGGRCMRWGP RERRALFLQA TPHRDISRRV AAFRFELHED QRAEMSPQAQ GLGVDGACRP CSDAELLLAA CTSDFVIHGT IHGVAHDTEL QESVITVVVA RVIRQTLPLF KEGSSEGQGR ASIRTLLRCG VRPGPGSFLF MGWSRFGEAW LGCAPRFQEF SRVYSAALTT HLNPCEMALD HHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Mannoside Acetylglucosaminyltransferase 2 Human Recombinant, Sf9

Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II.

Product # :

ENZ-1077

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Description

MGAT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 427 amino acids (30-447a.a.) and having a molecular mass of 49.3kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MGAT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

MGAT2 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 7.5), 10% glycerol, 0.15M NaCl and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.
Synonyms
Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADPRQRKNEA LAPPLLDAEP ARGAGGRGGD HPSVAVGIRR VSNVSAASLV PAVPQPEADN LTLRYRSLVY QLNFDQTLRN VDKAGTWAPR ELVLVVQVHN RPEYLRLLLD SLRKAQGIDN VLVIFSHDFW STEINQLIAG VNFCPVLQVF FPFSIQLYPN EFPGSDPRDC PRDLPKNAAL
KLGCINAEYP DSFGHYREAK FSQTKHHWWW KLHFVWERVK ILRDYAGLIL FLEEDHYLAP DFYHVFKKMW KLKQQECPEC DVLSLGTYSA SRSFYGMADK VDVKTWKSTE HNMGLALTRN AYQKLIECTD TFCTYDDYNW DWTLQYLTVS CLPKFWKVLV PQIPRIFHAG DCGMHHKKTC
RPSTQSAQIE SLLNNNKQYM FPETLTISEK FTVVAISPPR KNGGWGDIRD HELCKSYRRL QHHHHHH.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Endomucin Human Recombinant

Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.

Product # :

PRO-1156

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Description

EMCN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (19-190 a.a) and having a molecular mass of 20.5kDa.EMCN is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EMCN protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer, pH8.0, 10% glycerol, 1mM DTT and 100mM NaCl.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Endothelial sialomucin (Endomucin) interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix. Endomucin is expressed in the heart, kidney and lung.
Synonyms
Endomucin, Endomucin-2, Gastric cancer antigen Ga34, Mucin-14, MUC-14, EMCN, EMCN2, MUC14.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMNSTGV LEAANNSLVV TTTKPSITTP NTESLQKNVV TPTTGTTPKG TITNELLKMS LMSTATFLTS KDEGLKATTT DVRKNDSIIS NVTVTSVTLP NAVSTLQSSK PKTETQSSIK TTEIPGSVLQ PDASPSKTGT LTSIPVTIPE NTSQSQVIGT EGGKNASTSA TSRSYSS.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Galectin-16 Human Recombinant

Lectin Galactoside Binding Soluble 16, Galectin16, Galectin-16, LGALS-16, LGALS16.

Product # :

CYT-993

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Description

LGALS16 Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain having a molecular mass of 16kDa.The LGALS16 also appears as a homodimer and therefore a 32kDa band is observed as well. LGALS16 is fused to a 6xHis tag at n-terminal and purified using standard chromatography techniques.

Source

Escherichia Coli.

Formulation

1x PBS and 25mM arginine.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Galectin-16 (LGALS16) binds lactose with high affinity. LGALS16 is a strong inducer of T-cell apoptosis.
Synonyms
Lectin Galactoside Binding Soluble 16, Galectin16, Galectin-16, LGALS-16, LGALS16.
Physical Appearance
Sterile Filtered colorless solution.
Stability
The Recombinant LGALS16 protein although stable at 4°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Background
What is the molecular weight/Mw of LGALS16 HUMAN Protein?
LGALS16 HUMAN Protein has a total Mw of 16kDa.

What is the source or expression system of LGALS16 HUMAN Protein?
Escherichia Coli.

What is the Purity of LGALS16 HUMAN Protein?
LGALS16 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS16 HUMAN Protein?
The biological functionality of LGALS16 HUMAN Protein will be determined in the future.

What applications can LGALS16 HUMAN Protein be used in?
LGALS16 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for LGALS16 HUMAN Protein?
The endotoxin level is minimal, LGALS16 HUMAN Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Glyoxalase-I Human Recombinant, Active

GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.

Product # :

ENZ-999

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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biological activity
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Citations

Description

Glyoxalase-I Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 184 amino acids and having a molecular mass of 20.7 kDa. Glyoxalase-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Glyoxalase-1 solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Specific activity: > 400 units/mg. One unit will form 1.0umol of S-lactoylgutathione from methylglyoxal and reduced glutathione per minute at pH6.5 at 25C

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Introduction
GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.
Synonyms
GLYI, GLOD1, GLO1, Glyoxalase-1, Lactoylglutathione lyase, Methylglyoxalase, Aldoketomutase, Ketone-aldehyde mutase, Glyoxalase I, S-D-lactoylglutathione methylglyoxal lyase, Glx I.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MAEPQPPSGG LTDEAALSCC SDADPSTKDF LLQQTMLRVK DPKKSLDFYT RVLGMTLIQK CDFPIMKFSL YFLAYEDKND IPKEKDEKIAWALSRKATLE LTHNWGTEDD ETQSYHNGNS DPRGFGHIGI AVPDVYSACK RFEELGVKFV KKPDDGKMKG LAFIQDPDGY WIEILNPNKM ATLM.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

Description:

Endoglin Human Recombinant, His-Tag

CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

Product # :

CYT-823

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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sds-page
Citations

Description

Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.

Source

Escherichia Coli.

Formulation

The Endoglin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

sds-page

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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 64.9kDa.

What is the source or expression system of CD105 Protein?
Escherichia Coli.

What is the Purity of CD105 Protein?
CD105 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.

What is the amino acid sequence of CD105 Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG

What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 Protein was purified using conventional chromatography techniques.

ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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