Search: 1000 results found for "Neuropilin"

Description:

L-selectin Human Recombinant

L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.

Product # :

PRO-381

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Description

L-Selectin Human Recombinant is expressed in E. coli containing 294 amino acids 39-332 fused to an amino terminal hexahistidine tag, having a total molecular weight of 37.55kDa.

Source

Escherichia Coli.

Formulation

L-Sel is supplied in 1x PBS and 50% Glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.
Single band on Western Blot.

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Introduction
L-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. The L-Selectin molecule is composed of various domains: one homologous to lectins, one to epidermal growth factor, and two to the consensus repeat units found in C3/C4 binding proteins.
L-selectin is expressed constitutively on lymphocytes, monocytes and granulocytes and interacts specifically with carbohydrate groups on activated endothelial cells. L-Selectin may be shed by proteolytic cleavage and circulating levels in biological fluids may be used as an indicator of various pathological conditions. L-Selectin is cleaved by ADAM17.
L-selectin works as a "homing receptor" for leukocytes to enter secondary lymphoid tissues via the high endothelial venules. Ligands present on endothelial cells will attach to leukocytes expressing L-selectin, which causes the leukocytes to become localized at that juncture. The receptor is also located on the cell surfaces of "naive" T cells, which have not yet encountered their particular antigen. This surface expression is lost following the cells activation.
Synonyms
L-selectin, Lymph node homing receptor, Leukocyte adhesion molecule 1, LAM-1, Leukocyte surface antigen Leu-8, TQ1, gp90-MEL, Leukocyte-endothelial cell adhesion molecule 1, LECAM1, CD62 antigen-like family member L, CD62L antigen, LAM1, LNHR, LSEL, CD62L, LYAM1, Leu-8, PLNHR, hLHRc, Lyam-1, L-Sel.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 1-2 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
Applications
L-Selectin can be used directly as a positive control in Western blotting, ELISA, immunoprecipitation and other immunological experiments.
The biological activity of this product has not yet been tested.

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:

Canopy FGF Signaling Regulator 1 Human Recombinant

Protein canopy homolog 1, CNPY1.

Product # :

PRO-1872

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Description

CNPY1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids (1-92 a.a) and having a molecular mass of 13.3kDa. CNPY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CNPY1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Canopy FGF Signaling Regulator 1, also known as CNPY1, is expressed in the midbrain-hindbrain (MHB) boundary in zebrafish. CNPY1, which binds FGFR1, also takes part in FGF signaling.
Synonyms
Protein canopy homolog 1, CNPY1.
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 MGSMNDYKLE EDPVTKERTF KRFAPRKGDK IYQEFKKLYF YSDAYRPLKF ACETIIEEYE DEISSLIAQE THYLADKLCS EKSDLCETSA NHTEL.

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:

Nucleosome Assembly Protein 1-Like 1 Human Recombinant

Nucleosome assembly protein 1-like 1, NRP, hNRP, NAP1L, NAP1, NAP-1-related protein, HSP22-like protein interacting protein, MGC23410, MGC8688.

Product # :

PRO-985

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Description

NAP1L1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (1-388 a.a.) and having a molecular mass of 47.2kDa.NAP1L1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

NAP1L1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
NAP1L1 is a member of the nucleosome assembly protein (NAP) family. NAP1L1 protein plays a part in DNA replication, modulating chromatin formation and regulation of cell proliferation.
Synonyms
Nucleosome assembly protein 1-like 1, NRP, hNRP, NAP1L, NAP1, NAP-1-related protein, HSP22-like protein interacting protein, MGC23410, MGC8688.
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 MADIDNKEQS ELDQDLDDVE EVEEEETGEE TKLKARQLTV QMMQNPQILA ALQERLDGLV ETPTGYIESL PRVVKRRVNA LKNLQVKCAQ IEAKFYEEVH DLERKYAVLY QPLFDKRFEI INAIYEPTEE ECEWKPDEED EISEELKEKA KIEDEKKDEE KEDPKGIPEF WLTVFKNVDL LSDMVQEHDE PILKHLKDIK VKFSDAGQPM SFVLEFHFEP NEYFTNEVLT KTYRMRSEPD DSDPFSFDGP EIMGCTGCQI DWKKGKNVTL KTIKKKQKHK GRGTVRTVTK TVSNDSFFNF FAPPEVPESG DLDDDAEAIL AADFEIGHFL RERIIPRSVL YFTGEAIEDD DDDYDEEGEE ADEEGEEEGD EENDPDYDPK KDQNPAEC.

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:

Non-T-cell Activation Linker Human Recombinant

LAT2, Linker for Activation of T CellsFamily Member 2, HSPC046, LAB, WBSCR15, WBSCR5, WSCR5, Non-T-cell activation linker, Linker for activation of B-cells, Membrane-associated adapter molecule, Williams-Beuren syndrome chromosomal region 5 protein, Williams-Beuren syndrome chromosomal region 15 protein.

Product # :

PRO-827

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Description

NTAL Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (27-243 a.a.) and having a molecular mass of 26.2 kDa. NTAL protein is fused to a 21 amino acid His tag at N-terminus and is purified by standard chromatography.

Source

Escherichia Coli.

Formulation

NTAL Human solution containing 20mM Trsi HCL pH-8, & 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

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Introduction
NTAL participates in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. NTAL takes part in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2.
Synonyms
LAT2, Linker for Activation of T CellsFamily Member 2, HSPC046, LAB, WBSCR15, WBSCR5, WSCR5, Non-T-cell activation linker, Linker for activation of B-cells, Membrane-associated adapter molecule, Williams-Beuren syndrome chromosomal region 5 protein, Williams-Beuren syndrome chromosomal region 15 protein.
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 MRCSRPGAKR SEKIYQQRSL REDQQSFTGS RTYSLVGQAW PGPLADMAPT RKDKLLQFYP SLEDPASSRY QNFSKGSRHG SEEAYIDPIA MEYYNWGRFS KPPEDDDANS YENVLICKQK TTETGAQQEG IGGLCRGDLS LSLALKTGPT SGLCPSASPE EDEESEDYQN SASIHQWRES RKVMGQLQRE ASPGPVGSPD EEDGEPDYVN GEVAATEA.

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:

Sorcin Human Recombinant

Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.

Product # :

PRO-166

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Description

SRI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 221 amino acids (1-198 a.a.) and having a molecular mass of 24.1kDa. The SRI is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SRI solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.2M NaCl, 1mM DTT and 0.1mM PMSF.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Sorcin (SRI) which is a 22kDa calcium-binding protein was originally identified in multidrug-resistant cells. Sorcin, which modulates excitation-contraction coupling in the heart, contributes to calcium homeostasis in the heart sarcoplasmic reticulum.
Synonyms
Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.
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 MGSMAYPGHP GAGGGYYPGG YGGAPGGPAF PGQTQDPLYG YFAAVAGQDG QIDADELQRC LTQSGIAGGY KPFNLETCRL MVSMLDRDMS GTMGFNEFKE LWAVLNGWRQ HFISFDTDRS GTVDPQELQK ALTTMGFRLS PQAVNSIAKR YSTNGKITFD DYIACCVKLR ALTDSFRRRD TAQQGVVNFP YDDFIQCVMS V.

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:

TIAL1 Human Recombinant

TCBP, TIAR, TIA1 cytotoxic granule-associated RNA binding protein-like 1, TIA-1-related protein.

Product # :

PRO-2139

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Description

TIAL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-375 a.a) and having a molecular mass of 44.0kDa.TIAL1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

TIAL1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 50% glycerol, 2mM DTT and 1mM EDTA .

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TIAL1 belongs to a family of RNA-binding proteins, it has 3 RNA recognition motifs (RRMs), and binds adenine and uridine-rich elements in mRNA and pre-mRNAs of a extensive range of genes. TIAL1 regulates a variety of activities including translational control, splicing and apoptosis. TIAL1 different isoforms function differently with respect to post-transcriptional silencing.
Synonyms
TCBP, TIAR, TIA1 cytotoxic granule-associated RNA binding protein-like 1, TIA-1-related protein.
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 MGSMMEDDGQ PRTLYVGNLS RDVTEVLILQ LFSQIGPCKS CKMITEHTSN DPYCFVEFYE HRDAAAALAA MNGRKILGKE VKVNWATTPS SQKKDTSNHF HVFVGDLSPE ITTEDIKSAF APFGKISDAR VVKDMATGKS KGYGFVSFYN KLDAENAIVH MGGQWLGGRQ IRTNWATRKP PAPKSTQENN TKQLRFEDVV NQSSPKNCTV YCGGIASGLT DQLMRQTFSP FGQIMEIRVF PEKGYSFVRF STHESAAHAI VSVNGTTIEG HVVKCYWGKE SPDMTKNFQQ VDYSQWGQWS QVYGNPQQYG QYMANGWQVP PYGVYGQPWN QQGFGVDQSP SAAWMGGFGA QPPQGQAPPP VIPPPNQAGY GMASYQTQ.

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:

Glial-Derived Neurotrophic Factor Mouse Recombinant

ATF1, ATF2, HFB1-GDNF, GDNF.

Product # :

CYT-243

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Description

Glial derived Neurotrophic Factor Mouse Recombinant produced in E.Coli is a non-glycosylated homodimer containing 2 x 135 amino acids and having a total molecular mass of 30.2kDa. GDNF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDNF was lyophilized with no additives.

Purity

Greater than 98.0% as determined by analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

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Introduction
GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.
Synonyms
ATF1, ATF2, HFB1-GDNF, GDNF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF 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 Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.
Background
What is the molecular weight/Mw of GDNF MOUSE Protein?
GDNF MOUSE Protein has a total Mw of 30.2kDa.

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

What is the Purity of GDNF MOUSE Protein?
GDNF MOUSE Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GDNF MOUSE Protein?
The ED50 as determined by the dose-dependent proliferation of C6 cells, is 0.8-0.12µg/ml.

What is the amino acid sequence of GDNF MOUSE Protein?
MSPDKQAAL PRRENRNRQAA AASPENSRGK GRRGQRGKNR GCVLTAIHLN VTDLGLGYET KEELIFRYCS GSCESAETMY DKILKNLSRS RRLTSDKVGQ ACCRPVAFDD DLSFLDDNLV YHILRKHSAK RCGCI.
What applications can GDNF MOUSE Protein be used in?
GDNF MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDNF MOUSE Protein?
The endotoxin level is minimal, GDNF MOUSE 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:

Cyclophilin-B Mouse Recombinant

Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.

Product # :

ENZ-1039

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Description

Cyclophilin B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (34-216 a.a) and having a molecular mass of 22.7kDa.Cyclophilin B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Cyclophilin B protein solution (1mg/ml) containing Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 1,000 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-PNA per minute at 37C in Tris–HCl pH 8.0 using chymotrypsin.

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Introduction
Cyclophilin B (also known as PPIB, peptidylpropyl isomerase B) is a cyclosporine-binding protein and is mainly located within the endoplasmic reticulum. It is associated with the secretory pathway and released in biological fluids. This protein can bind to cells derived from T- and B-lymphocytes, and may regulate cyclosporine A-mediated immunosuppression.
Synonyms
Peptidyl-prolyl cis-trans isomerase B, PPIase B, CYP-S1, Cyclophilin B, Rotamase B, S-cyclophilin, SCYLP.
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 MGSMNDKKKG PKVTVKVYFD LQIGDESVGR VVFGLFGKTV PKTVDNFVAL ATGEKGFGYK NSKFHRVIKD FMIQGGDFTR GDGTGGKSIY GERFPDENFK LKHYGPGWVS MANAGKDTNG SQFFITTVKT SWLDGKHVVF GKVLEGMDVV RKVESTKTDS
RDKPLKDVII VDSGKIEVEK PFAIAKE.

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:

Resistin (64-110) Human Recombinant

Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.

Product # :

CYT-1232

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Description

The Resistin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Resistin His-Tagged Fusion Protein, produced in E. coli, is a 12kDa protein containing 47 amino acid residues of the Resistin Human, 64-110 amino acids.

Source

Escherichia Coli.

Formulation

Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.

Purity

Greater than 80% as determined by SDS-PAGE.

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Synonyms
Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized Resistin at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
Solubility
It is recommended to 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 on cell culture.
Background
Human resistin is an adipokine primarily secreted by adipose tissue, mainly in response to obesity and inflammatory conditions.
Resistin Function
Resistin takes part in insulin resistance, which can be the cause of the development of type 2 diabetes. Resistin can also affect glucose metabolism and insulin signalling.
Regulation
Levels of resistin are influenced by factors such as inflammation, obesity and certain hormones. It tends to increase in conditions associated with obesity and metabolic syndrome.
Clinical Relevance
Elevated levels of resistin have been associated with obesity-related conditions, cardiovascular diseases, and metabolic disorders. Resisting is considered as a potential biomarker for these conditions.
Resistin Mechanism
Resistin promotes insulin resistance through different pathways such as the modulation of inflammatory processes and the inhibition of insulin signaling in target tissues like liver and muscle.
Research
Ongoing studies are exploring resistin’s role in metabolic regulation, the exact mechanisms of action of resistin and its potential as a therapeutic target for treating metabolic diseases.
Overall, resistin is a critical factor in metabolic health, mainly in the context of diabetes and obesity.

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

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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.

Description:

Insulin Human Recombinant, His Tag

Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.

Product # :

CYT-1076

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Description

Insulin Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (25-110 a.a) and having a molecular mass of 11.8kDa. Insulin is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Insulin protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured in a cell proliferation assay using MCF7 human breast cancer cell. The ED50 for this effect is less or equal to 4 ug/ml.

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Introduction
Insulin decreases blood glucose concentration. it increases cell permeability to monosaccharides, amino acids and fatty acids. it accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
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 MGSFVNQHLC GSHLVEALYL VCGERGFFYT PKTRREAEDL QVGQVELGGG PGAGSLQPLA LEGSLQKRGI VEQCCTSICS LYQLENYCN

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-3 Mouse Recombinant, BioActive

Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.

Product # :

CYT-1151

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Description

LGALS3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids ( 1-264 a.a) and having a molecular mass of 29.8kDa.LGALS3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

LGALS3 protein (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 50% glycerol,1mM DTT and 2mM EDTA.

Purity

Greater than 95% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

sds-page

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Introduction
Galectin 3, or LGALS3, is a protein which belongs to the animal lectins family, that binds betagalactoside residues selectively. LGALS3 is originated and leaves cells through ectocytosis. The protein is capable of inhibition apoptosis and the development of cancer. Galectin 3 is found in epithelial tissues in organisms, it can be located in dendritic cells, Kupffer cells, macrophages etc. LGALS3 levels elevated when inflammation is generating, cell proliferation, trans-activation by viral proteins and cell differentiation.
Synonyms
Lectin galactose binding soluble 3, Lectin, galactose binding, soluble 3, CBP35, GAL3, GALBP, GALIG, LGALS2, MAC2.
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 MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.
Background
What is the molecular weight/Mw of LGALS3 MOUSE Protein?
LGALS3 MOUSE Protein has a total Mw of 29.8kDa.

What is the source or expression system of LGALS3 MOUSE Protein?
Escherichia Coli.

What is the Purity of LGALS3 MOUSE Protein?
LGALS3 MOUSE Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of LGALS3 MOUSE Protein?
Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml.

What is the amino acid sequence of LGALS3 MOUSE Protein?
MGSSHHHHHH SSGLVPRGSH MGSMADSFSL NDALAGSGNP NPQGYPGAWG NQPGAGGYPG AAYPGAYPGQ APPGAYPGQA PPGAYPGQAP PSAYPGPTAP GAYPGPTAPG AYPGSTAPGA FPGQPGAPGA YPSAPGGYPA AGPYGVPAGP LTVPYDLPLP GGVMPRMLIT IMGTVKPNAN RIVLDFRRGN DVAFHFNPRF NENNRRVIVC NTKQDNNWGK EERQSAFPFE SGKPFKIQVL VEADHFKVAV NDAHLLQYNH RMKNLREISQ LGISGDITLT SANHAMI.

What applications can LGALS3 MOUSE Protein be used in?
LGALS3 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

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:

Activin A Receptor Type II-Like 1 Human Recombinant

Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.

Product # :

CYT-920

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Description

ACVRL1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 103 amino acids (22-118a.a.) and having a molecular mass of 11.5kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa).ACVRL1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

ACVRL1 protein solution (0.25mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Activin A Receptor Type II-Like 1, ACVRLK1, ALK1, TGF-B Superfamily Receptor Type I EC 2.7.11.30, TSR-I, ALK-1, HHT2, SKR3 Serine/Threonine-Protein Kinase Receptor R3 Activin A Receptor, Type II-Like Kinase 1, Activin Receptor-Like Kinase 1, EC 2.7.11, ORW2, HHT.
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
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.
Background
The Physiological Implications and Therapeutic Potential of Activin A Receptor Type II-Like 1 Human Recombinant
1. Abstract
This research paper investigates the Activin A Receptor Type II-Like 1 Human Recombinant (ACVRL1), a significant protein involved in the TGF-beta superfamily signaling pathway. We provide an extensive understanding of ACVRL1’s structure, signaling mechanism, biological functions, and implications in disease pathology. Additionally, we explore the therapeutic potential of ACVRL1 in various pathological conditions.
2. Introduction
ACVRL1, also known as ALK1, plays an essential role in the TGF-beta signaling pathway, which has implications in cellular proliferation, differentiation, and apoptosis. Understanding ACVRL1 and its signaling mechanisms could provide insights into its potential therapeutic applications in various diseases.
3. Structure and Signaling of ACVRL1
ACVRL1 is a type I receptor protein involved in the TGF-beta signaling pathway. It is a transmembrane protein that consists of a ligand-binding extracellular domain and an intracellular domain responsible for signal transduction. Binding of ligands to ACVRL1 triggers phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVRL1
ACVRL1 plays pivotal roles in multiple biological processes, including vascular development, angiogenesis, and maintenance of vascular integrity. It is known to influence cellular processes such as proliferation, differentiation, and apoptosis, thereby implicating it in organogenesis and homeostasis.
5. ACVRL1 in Disease Pathology
Mutations in the ACVRL1 gene have been associated with hereditary hemorrhagic telangiectasia (HHT), a genetic disorder characterized by abnormal blood vessel formation. This link underscores the critical role of ACVRL1 in vascular biology and disease.
6. Therapeutic Potential of ACVRL1
Given its crucial role in vascular biology and its link to HHT, ACVRL1 presents a promising target for therapeutic interventions. Modulation of ACVRL1 signaling could potentially provide treatment options for pathological conditions related to abnormal blood vessel formation and function.
7. Conclusion and Future Perspectives
Our understanding of ACVRL1 and its functions has grown significantly in recent years, but there is much yet to be discovered. Continued research into ACVRL1's precise molecular mechanisms and its roles in disease will undoubtedly open new doors for therapeutic developmen
What is the molecular weight / Mw of ACVRL1 Protein?
ACVRL1 Protein has a total Mw of 11.5kDa.
What is the source or expression system of ACVRL1 Protein?
Sf9, Insect cells.

What is the Purity of ACVRL1 Protein?
ACVRL1 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of ACVRL1 Protein?
The biological functionality of ACVRL1 Protein will be determined in the future.

What is the amino acid sequence of ACVRL1 Protein?
DPVKPSRGPL VTCTCESPHC KGPTCRGAWC TVVLVREEGR HPQEHRGCGN LHRELCRGRP TEFVNHYCCD SHLCNHNVSL VLEATQPPSEQPGTDGQHHH HHH.

What applications can ACVRL1 Protein be used in?
ACVRL1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for ACVRL1 Protein?
The endotoxin level is minimal, ACVRL1 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:

Serpin Peptidase Inhibitor, Clade B Member 2 Human Recombinant

Serpin Peptidase Inhibitor Clade B (Ovalbumin) Member 2, Serine (Or Cysteine) Proteinase Inhibitor Clade B (Ovalbumin) Member 2, Placental Plasminogen Activator Inhibitor, Plasminogen Activator Inhibitor Type II (Arginine-Serpin), PAI2, PLANH2, Monocyte Arg-Serpin, Serpin B2, HsT1201, PAI.

Product # :

PRO-1788

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Description

SERPINB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 415 amino acids and having a molecular mass of 46.6kDa.The SERPINB2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH8.0, 150mM NaCl, 1mM Cysteine, with 5% Trehalose.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The biologically active was determined by its inhibitory effect against single chain tPA induced cleavage of a chromogenic substrate in Imidazole Buffer at 37°C. Half maximal inhibition against 1.0 µg/ml of single chain tPA was at a concentration of 1.0µg/ml.

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Introduction
SERPINB2 is an inhibitory serpin produced primarily in keratinocytes, stimulated monocytes, and placental trophoblasts. SERPINB2 is found primarily as a 47 kDa non-glycosylated intracellular protein that is induced to be secreted as 60 kDa glycoprotein. The glycosylated and unglycosylated SERPINB2 are similarly effective as inhibitors of uPA, the only proven physiological target of SERPINB2.
Synonyms
Serpin Peptidase Inhibitor Clade B (Ovalbumin) Member 2, Serine (Or Cysteine) Proteinase Inhibitor Clade B (Ovalbumin) Member 2, Placental Plasminogen Activator Inhibitor, Plasminogen Activator Inhibitor Type II (Arginine-Serpin), PAI2, PLANH2, Monocyte Arg-Serpin, Serpin B2, HsT1201, PAI.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SERPINB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SERPINB2 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 SERPINB2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MEDLCVANTL FALNLFKHLA KASPTQNLFL SPWSISSTMA MVYMGSRGST EDQMAKVLQF NEVGANAVTP MTPENFTSCG FMQQIQKGSY PDAILQAQAA DKIHSSFRSL SSAINASTGN YLLESVNKLF GEKSASFREE YIRLCQKYYS SEPQAVDFLE CAEEARKKIN SWVKTQTKGK IPNLLPEGSV DGDTRMVLVN AVYFKGKWKT PFEKKLNGLY PFRVNSAQRT PVQMMYLREK LNIGYIEDLK AQILELPYAG DVSMFLLLPD EIADVSTGLE LLESEITYDK LNKWTSKDKM AEDEVEVYIP QFKLEEHYEL RSILRSMGME DAFNKGRANF SGMSERNDLF LSEVFHQAMV DVNEEGTEAA AGTGGVMTGR TGHGGPQFVA DHPFLFLIMH KITNCILFFG RFSSP

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:

Serpin Peptidase Inhibitor, Clade B Member 4 Human Recombinant

SERPINB4, Serpin Peptidase Inhibitor, Clade B (Ovalbumin), Member, Squamous Cell Carcinoma, Antigen, SCCA2, Serine (Or Cysteine) Proteinase Inhibitor, Clade B (Ovalbumin), Member, Peptidase Inhibitor, LEUPIN, SCCA, PI11, Protease Inhibitor (Leucine-Serpin) Squamous Cell Carcinoma Antigen, SCCA2/SCCA1 Fusion Protein, Serpin B4, SCCA1 PI-11.

Product # :

PRO-2208

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Description

SERPINB4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 413 amino acids (1-390 a.a) and having a molecular mass of 47.2kDa.SERPINB4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SERPINB4 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Serpin Peptidase Inhibitor, Clade B Member 4, also known as SERPINB4 is a member of the serpin family. SERPINB4 acts as a protease inhibitor to modulate the host immune response against tumor cells. Among the diseases associated with SERPINB4 are: inverted papilloma as well as burns.
Synonyms
SERPINB4, Serpin Peptidase Inhibitor, Clade B (Ovalbumin), Member, Squamous Cell Carcinoma, Antigen, SCCA2, Serine (Or Cysteine) Proteinase Inhibitor, Clade B (Ovalbumin), Member, Peptidase Inhibitor, LEUPIN, SCCA, PI11, Protease Inhibitor (Leucine-Serpin) Squamous Cell Carcinoma Antigen, SCCA2/SCCA1 Fusion Protein, Serpin B4, SCCA1 PI-11.
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 MGSMEDLCVA NTLFALNLFK HLAKASPTQN LFLSPWSISS TMAMVYMGSR GSTEDQMAKV LQFNEVGANA VTPMTPENFT SCGFMQQIQK GSYPDAILQA QAADKIHSSF RSLSSAINAS TGNYLLESVN KLFGEKSASF REEYIRLCQK YYSSEPQAVD FLECAEEARK KINSWVKTQT KGKIPNLLPE GSVDGDTRMV LVNAVYFKGK WKTPFEKKLN GLYPFRVNSA QRTPVQMMYL REKLNIGYIE DLKAQILELP YAGDVSMFLL LPDEIADVST GLELLESEIT YDKLNKWTSK DKMAEDEVEV YIPQFKLEEH YELRSILRSM GMEDAFNKGR ANFSGMSERN DLFLSEVFHQ AMVDVNEEGT EAAAGTGGVM TGRTGHGGPQ FVADHPFLFL IMHKITNCIL FFGRFSSP.

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:

Neurotensin Human Recombinant, sf9

Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.

Product # :

PRO-2374

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Description

NTS Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 134 amino acids (24-148) and having a molecular mass of 15.4kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa).NTS is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

NTS protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by analysis by SDS-PAGE.

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Introduction
Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in dopamine-associated pathophysiological events, in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.
Synonyms
Neurotensin/neuromedin N, NTS, Neuromedin N, NN, NmN, NT, NmN-125.
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
ADPSDSEEEM KALEADFLTN MHTSKISKAH VPSWKMTLLN VCSLVNNLNS PAEETGEVHE EELVARRKLP TALDGFSLEA MLTIYQLHKI CHSRAFQHWE LIQEDILDTG NDKNGKEEVI KRKIPYILHH HHHH.

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:

Oligodendrocyte Myelin Glycoprotein Recombinant Human

Oligodendrocyte-myelin glycoprotein, OMG, OMGP.

Product # :

PRO-2343

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Description

OMG Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 401 amino acids (25-418) and having a molecular mass of 45.4kDa (Molecular size on SDS-PAGE will appear at approximately 50-100kDa).OMG is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

OMG protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by analysis by SDS-PAGE.

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Introduction
Oligodendrocyte-myelin glycoprotein (OMG) is a cell membrane protein which contains 8 leucine-rich repeats. The OMG protein is expressed on the surface of oligodendrocytes and on large projection neurons, including Purkinje cells of the cerebellum, pyramidal cells of the hippocampus, motoneurons of the brainstem and anterior horn cells of the spinal cord. The neurite outgrowth inhibitory activities of all three myelin-derived proteins are mediated by binding to a joint receptor complex consisting of the Nogo receptor and the p75 neurotrophin receptor.
Synonyms
Oligodendrocyte-myelin glycoprotein, OMG, OMGP.
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
ICPLQCICTE RHRHVDCSGR NLSTLPSGLQ ENIIHLNLSY NHFTDLHNQL TQYTNLRTLD ISNNRLESLP AHLPRSLWNM SAANNNIKLL DKSDTAYQWN LKYLDVSKNM LEKVVLIKNT LRSLEVLNLS SNKLWTVPTN MPSKLHIVDL SNNSLTQILP GTLINLTNLT HLYLHNNKFT FIPDQSFDQL FQLQEITLYN NRWSCDHKQN ITYLLKWMME TKAHVIGTPC STQISSLKEH NMYPTPSGFT SSLFTVSGMQ TVDTINSLSV VTQPKVTKIP KQYRTKETTF GATLSKDTTF TSTDKAFVPY PEDTSTETIN SHEAAAATLT IHLQDGMVTN TSLTSSTKSS PTPMTLSITS GMPNNFSEMP QQSTTLNLWR EETTTNVKTP LPSVEHHHHH H.

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:

Follistatin Mouse Recombinant

Follistatin, FST, FS, Activin-binding protein, AL033346.

Product # :

CYT-124

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Shipped at Room temp

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Description

Follistatin Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 289 amino acids and having a total molecular mass of 31.6kDa.The FST is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Mouse Follistatin is lyophilized from 10mM Na2PO4 and 50mM NaCl, pH 7.5.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.

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Introduction
Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin binds directly to activin and functions as an activin antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).
Synonyms
Follistatin, FST, FS, Activin-binding protein, AL033346.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.
Background
What is the molecular weight/Mw of FOLLISTATIN MOUSE Protein?
FOLLISTATIN MOUSE Protein has a total Mw of 31.6kDa.

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

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

What is the Biological Activity of FOLLISTATIN MOUSE Protein?
The ED50, determined by the dose-dependent neutralization of 7.5ng/ml human Activin-A on MCP-11 cells, is 0.13-0.19µg/ml.

What is the amino acid sequence of FOLLISTATIN MOUSE Protein?
MGNCWLRQAK NGRCQVLTKT ELSKEECCST GRLSTSWTEE DVNDNTLFKW MIFNGGAPNC IPCKETCENV DCGPGKKCRM NKKNKPRCVC APDCSNITWK GPVCGLDGKT YRNECALLKA RCKEQPELEV QYQGRCKKTC RDVFCPGSST CVVDQTNNAY CVTCNRICPE PASSEQYLCG NDGVTYSSAC HLRKATCLLG RSIGLAYEGK CIKAKSCEDI QCTGGKKCLW DS.

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

What is the endotoxin level for FOLLISTATIN MOUSE Protein?
The endotoxin level is minimal, FOLLISTATIN MOUSE 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:

Follistatin Like 1 Human Recombinant, HEK

Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.

Product # :

CYT-1027

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Quantity :

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Shipped at Room temp

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Description

FSTL1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-308) containing 296 amino acids including a 8 a.a C-terminal His tag. The total molecular mass is 33.8kDa (calculated).

Source

HEK293 cells.

Formulation

FSTL1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline and 5 % (w/v) trehalose, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
FSTL1 protein resembles follistatin, an activin-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.
Synonyms
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. 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
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. FSTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
Amino Acid Sequence
EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.
Background
What is the molecular weight/Mw of FSTL1 HUMAN, HEK Protein?
FSTL1 HUMAN, HEK Protein has a total Mw of 33.8kDa.

What is the source or expression system of FSTL1 HUMAN, HEK Protein?
HEK293 cells.

What is the Purity of FSTL1 HUMAN, HEK Protein?
FSTL1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FSTL1 HUMAN, HEK Protein?
The biological functionality of FSTL1 HUMAN, HEK Protein will be determined in the future.

What is the amino acid sequence of FSTL1 HUMAN, HEK Protein?
EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.

What applications can FSTL1 HUMAN, HEK Protein be used in?
FSTL1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FSTL1 HUMAN, HEK Protein?
The endotoxin level is minimal, FSTL1 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:

Glycophorin A Human Recombinant

Glycophorin A (MNS Blood Group), Glycophorin A (MN Blood Group), Sialoglycoprotein Alpha, MN Sialoglycoprotein, PAS-2, GPA, Erythroid-Lineage-Specific Membrane Sialoglycoprotein, Recombinant Glycophorin A-B Miltenberger-DR, Glycophorin A (Includes MN Blood Group), Mi.V Glycoprotein (24 AA), Glycophorin Sta Type C, Glycophorin A, GPA, Glycophorin Erik, Glycophorin MiV, Glycophorin SAT, CD235a Antigen, Glycophorin-A, HGpSta(C), HGpMiXI, CD235a, GPErik, HGpMiV, GPSAT, MNS, MN.

Product # :

PRO-2426

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

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Description

GYPA Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 81 amino acids (20-91a.a.) and having a molecular mass of 9.1kDa. (Molecular size on SDS-PAGE under reducing conditions 18-28kDa).GYPA is expressed with a 9 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

GYPA protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

More Info

Introduction
Glycophorins A & B (GYPA &GYPB) are the main sialoglycoproteins of the human erythrocyte membrane which carry the antigenic determinants for the MN and Ss blood groups. Along with the M or N and S or s antigens which normally occur in all populations, approximately 40 related variant phenotypes were identified. These variants comprise all the variants of the Miltenberger complex and some isoforms of Sta, as well as Dantu, Sat, He, Mg, and deletion variants Ena, S-s-U- and Mk. GYPA is significant for the function of SLC4A1 and is necessary for high activity of SLC4A1. GYPA is involved in translocation of SLC4A1 to the plasma membrane. GYPA is also a receptor for: the influenza virus, Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans and is also a receptor for Hepatitis A virus (HAV).
Synonyms
Glycophorin A (MNS Blood Group), Glycophorin A (MN Blood Group), Sialoglycoprotein Alpha, MN Sialoglycoprotein, PAS-2, GPA, Erythroid-Lineage-Specific Membrane Sialoglycoprotein, Recombinant Glycophorin A-B Miltenberger-DR, Glycophorin A (Includes MN Blood Group), Mi.V Glycoprotein (24 AA), Glycophorin Sta Type C, Glycophorin A, GPA, Glycophorin Erik, Glycophorin MiV, Glycophorin SAT, CD235a Antigen, Glycophorin-A, HGpSta(C), HGpMiXI, CD235a, GPErik, HGpMiV, GPSAT, MNS, MN.
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
ADPLSTTEVA MHTSTSSSVT KSYISSQTND THKRDTYAAT PRAHEVSEIS VRTVYPPEEE TGERVQLAHH FSEPEHHHHH H

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:

Glycophorin C Human Recombinant

Glycophorin C (Gerbich Blood Group), Sialoglycoprotein D, Glycoprotein Beta, Glycoconnectin, Glycophorin-D, PAS-2, GPD 3 4, GPC, Glycophorin-C, CD236 Antigen, CD236R, CD236, GYPD, GLPC, GE, Glycophorin-C, Glycoconnectin, Glycophorin-D, GPD, Glycoprotein beta, PAS-2', Sialoglycoprotein D.

Product # :

PRO-2408

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Shipping Method :

Shipped with Ice Packs

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Description

GYPC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 66 amino acids (1-57a.a.) and having a molecular mass of 7.2kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). GYPC is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

GYPC protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Glycophorin C, also known as GYPC, is an integral membrane glycoprotein. GYPC is a minor species which is carried by human erythrocytes, however plays an important role in regulating the mechanical stability of red cells. Numeral glycophorin C mutations have been described. The Gerbich and Yus phenotypes are due to deletion of exon 3 & 2, respectively. The Webb & Duch antigens, also identified as glycophorin D, result from single point mutations of the glycophorin C gene. The glycophorin C protein has very slight homology with glycophorins A & B.
Synonyms
Glycophorin C (Gerbich Blood Group), Sialoglycoprotein D, Glycoprotein Beta, Glycoconnectin, Glycophorin-D, PAS-2, GPD 3 4, GPC, Glycophorin-C, CD236 Antigen, CD236R, CD236, GYPD, GLPC, GE, Glycophorin-C, Glycoconnectin, Glycophorin-D, GPD, Glycoprotein beta, PAS-2', Sialoglycoprotein D.
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
ADPMWSTRSP NSTAWPLSLE PDPGMASAST TMHTTTIAEP DPGMSGWPDG RMETSTPTIM 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:

Cetrorelix

Product # :

HOR-277

Price :

Quantity :

Shipping Method :

Shipped at Room temp

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Description

Cetrorelix acetate is a synthetic decapeptide with gonadotropin-releasing hormone (GnRH) antagonistic activity. Cetrorelix acetate is an analog of native GnRH with substitutions of amino acids at positions 1, 2, 3, 6, and 10. The molecular formula is C70H92CIN17O14 (Ac-D-Nal1-D-Cpa2-D-Pal3-Ser4-Tyr5- D-Cit6-Leu7-Arg8-Pro9-D -Ala10-NH2), and the molecular weight is 1431 Dalton, calculated as the anhydrous free base.

Formulation

The Cetrorelix peptide was lyophilized with no additives.

Purity

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

More Info

Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Cetrorelix although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cetrorelix 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 Cetrorelix in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of CETRORELIX Protein?
CETRORELIX Protein has a total Mw of 1.4kDa.

What is the Purity of CETRORELIX Protein?
CETRORELIX Protein is > 98% pure as determined by SDS-PAGE.

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

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

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

Who supplies CETRORELIX that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CETRORELIX?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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:

Gamma-Synuclein Human Recombinant

Gamma-synuclein, Persyn, Breast cancer-specific gene 1 protein, Synoretin, SR, SNCG, BCSG1, PERSYN, PRSN, g-Synuclein.

Product # :

PRO-395

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Shipping Method :

Shipped with Ice Packs

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Description

g-Synuclein Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 13,300 Dalton. The protein coding region of g-synuclein was amplified by RT-PCR and cloned into an E.coli expression vector. g-synuclein was overexpressed in E. coli and purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) contains 20mM Tris-HCl buffer (pH 7.5) and 0.1M NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
g-synuclein(Originally known as a breast cancer specific gene product, BCSG1) is an acidic neuronal protein of 127 amino acids. Gamma-Synuclein is a member of the Synuclein protein family, which is believed to be involved in the pathogenesis of neurodegenerative diseases. High levels of Gamma-Synuclein have been found in advanced breast carcinomas suggesting a correlation between overexpression of SNCG and breast tumor development. Synuclein-Gamma is found mostly in the peripheral nervous system (in primary sensory neurons, sympathetic neurons, and motor neurons) and retina. SNCG is also identified in the brain, ovarian tumors, and in the olfactory epithelium. SNCG expression in breast tumors is a marker for tumor progression. A modification in the expression of gamma-synuclein has been detected in the retina of Alzheimer's patients.
Synonyms
Gamma-synuclein, Persyn, Breast cancer-specific gene 1 protein, Synoretin, SR, SNCG, BCSG1, PERSYN, PRSN, g-Synuclein.
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
MDVFKKGFSI AKEGVVGAVE KTKQGVTEAA EKTKEGVMYV GAKTKENVVQSVTSVAEKTK EQANAVSEAV VSSVNTVATK TVEEAENIAV TSGVVRKEDL RPSAPQQEGV ASKEKEEVAE EAQSGGD.

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:

Batroxobin

Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.

Product # :

PRO-2146

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Quantity :

Shipping Method :

Shipped at Room temp

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Description

Batroxobin, isolated from Bothrops atrox snake venom, has an Mw of approximately 43kDa.

Formulation

The Batroxobin protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

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Introduction
Batroxobin is a serin protease that reduces fibronogen levels and is originally extracted from snake venom of Bothrops Atrox. Batroxobin is used in defibrinogenation and thrombolysis and also has an effect on c-fos gene and growth factor.
Batroxobin can efficiently restrain proliferation of VSMCs, by blocking the release and uptake of Ca2+, thus influencing [Ca2+]i.
Batroxobin converts fibrinogen to fibrin through the restricted release of fibrinopeptide-A from fibrinogen to promote blood to clot. Unlike thrombin, it is not affected by heparin and hirudin.
Synonyms
Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.
Physical Appearance
Sterile Filtered white lyophilized powder.
Stability
Store the lyophilized Batroxobin between 2-8°C. Do not freeze!
Solubility
It is recommended to reconstitute the lyophilized Batroxobin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.
Unit Definition
100BU [Batroxobin Units]=1mg.

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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