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1000 results found for “calcium binding protein”
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Name :
THRSP HumanDescription:
Thyroid Hormone Responsive Human Recombinant
Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 protein.
Product # :
PRO-1485Price :
Quantity :
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Shipped with Ice Packs
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Description
THRSP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146 a.a.) and having a molecular mass of 18.9kDa.THRSP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
THRSP protein solution (1mg/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.
More Info
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Introduction
Thyroid Hormone Responsive (THRSP) is a member of the SPOT14 family. THRSP is similar to the gene product of S14, a rat gene whose expression is limited to liver and adipose tissue and is controlled by nutritional and hormonal factors. THRSP is expressed in liver and adipocytes, specifically in lipomatous modules. In addition It is expressed in lipogenic breast cancers, which suggests a role in controlling tumor lipid metabolism.
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Synonyms
Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 protein.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMQVLTKR YPKNCLLTVM DRYAAEVHNM EQVVMIPSLL RDVQLSGPGG QAQAEAPDLY TYFTMLKAIC VDVDHGLLPR EEWQAKVAGS EENGTAETEE VEDESASGEL DLEAQFHLHF SSLHHILMHL TEKAQEVTRK YQEMTGQVW.
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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Name :
GDF11 Human, HisDescription:
Growth and Differentiation factor 11 Human Recombinant, His Tag
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
Product # :
CYT-887Price :
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Description
GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.
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Synonyms
Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
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Background
What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.
What is the source or expression system of GDF11 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF11 HUMAN, HIS Protein?
GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF11 HUMAN, HIS Protein?
The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.
What applications can GDF11 HUMAN, HIS Protein be used in?
GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GDF11 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF11 HUMAN, HIS 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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Name :
SIVA1 HumanDescription:
SIVA1 Human Recombinant
Apoptosis regulatory protein Siva isoform 1, Apoptosis regulatory protein Siva, CD27-binding protein, CD27BP, SIVA, SIVA1, Siva-1, Siva-2
Product # :
PRO-2652Price :
Quantity :
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Shipped with Ice Packs
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Description
SIVA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (1-175 a.a.) and having a molecular mass of 21.1 kDa. SIVA1 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SIVA1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
SIVA1, also referred to asApoptosis regulatory protein Siva isoform 1, is a death domain-containing proapoptotic protein. It is known as glucocorticoid-induced TNFR family-related gene, and also as an intracellular ligand of CD27, which are both members of the TNFR family expressed on lymphoid cells. There isn’t much known about the signalling pathway underlying the Siva-induced apoptosis.SIVA1 expression is modulated in multiple pathological processes.
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Synonyms
Apoptosis regulatory protein Siva isoform 1, Apoptosis regulatory protein Siva, CD27-binding protein, CD27BP, SIVA, SIVA1, Siva-1, Siva-2
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPKRSCP FADVAPLQLK VRVSQRELSR GVCAERYSQE VFEKTKRLLF LGAQAYLDHV WDEGCAVVHL PESPKPGPTG APRAARGQML IGPDGRLIRS LGQASEADPS GVASIACSSC VRAVDGKAVC GQCERALCGQ CVRTCWGCGS VACTLCGLVD CSDMYEKVLC TSCAMFET
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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Name :
Tpc1808 RatDescription:
Tropic 1808 Rat Recombinant
Tropic 1808, Tpc1808.
Product # :
PRO-587Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Tropic-1808 Rat Recombinant protein fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids and having a molecular mass of 29.1 kDa.The Tpc1808 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Tropic-1808 was lyophilized from 1X PBS, pH 7.4.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Tropic 1808 is a candidate chemotropic factor induced by nerve injury. Tpc1808 protein, similar to NGF, could promote the expression of NF-H in a time-dependent manner. Tpc1808 is the gene related to promotion of nerve growth, and both the Tpc1808 gene and the Tpc1808 recombinant protein up-regulate the expression of NF-H in PC12 cells.
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Synonyms
Tropic 1808, Tpc1808.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Tpc1808 although stable 10°C for 1 week, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.
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Amino Acid Sequence
MSYYHHHHHHMNLAQIAALNQISNLNAIRVGQVLKVSNAAGSNNTQNTTQPS
AGVPTNTASSTTGYTVKSGDTLSAIAAANGVSLANLLSWNNLSLQAIIYPGQKL
TIQNANNATVTTPNAPTSTPTVMPSTNGSYTVKSGDTLYGIAAKLGTNVQTLLS
LNGLQLSSTIYVGQVLKTTGAVAGAGTATSTPTPVTPTVSKPAAANGVSTAGLS
AAQAAWLRTAVVDAQAATAGTGVLASVTVAQAILESGWGQSALASAPYHNF
NLYLIKVKNTWKLMTLLLS.
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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Name :
CFB-a HumanDescription:
Complement Factor B Fragment a Human
Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.
Product # :
PRO-2735Price :
Quantity :
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Shipped with Ice Packs
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Description
CFB-a Human produced in Human Plasma having a molecular mass of 33 kDa.
Source
Human Plasma.
Formulation
CFB-a solution (1mg/ml) contains Phosphate-buffered saline, pH 7.2.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.
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Synonyms
Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.
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Physical Appearance
Sterile filtered solution.
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Stability
CFB-a Human is stable at 4°C if entire vial will be used within 2-4 weeks. Store, frozen below -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.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.
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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Name :
CETN3 HumanDescription:
Centrin-3 Human Recombinant
CEN3, CEN-3, CETN-3.
Product # :
PRO-533Price :
Quantity :
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Shipped with Ice Packs
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Description
CETN3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.7 kDa. CETN3 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
CETN3 Human 0.5mg/ml solution contains 20mM Trsi HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CETN3 comprises of 4 EF-hand calcium binding domains, and is a part of the centrin protein family. CETN3 protein is widely expressed cytoskeletal components that demonstrate increased expression during cell differentiation. CETN3 takes part in centrosome reproduction.
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Synonyms
CEN3, CEN-3, CETN-3.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSLALRSELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDEAIDYHEL KVAMRALGFD VKKADVLKIL
KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI
AIMTGDI.
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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Name :
PCBP1 HumanDescription:
Poly (RC) Binding Protein 1 Human Recombinant
Poly(rC) binding protein 1, hnRNP-E1, hnRNP-X, HNRPE1, HNRPX, Alpha-CP1, Heterogeneous nuclear ribonucleoprotein E1, Nucleic acid-binding protein SUB2.3, PCBP1.
Product # :
PRO-1690Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PCBP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-163) and having a molecular mass of 19.6 kDa.PCBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PCBP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
PCBP1 is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. PCBP1 plays a role in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability. PCBP1 along with PCBP-2 and hnRNPK corresponds to the major cellular poly(rC)-binding protein. PCBP1 and PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promotes poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure.
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Synonyms
Poly(rC) binding protein 1, hnRNP-E1, hnRNP-X, HNRPE1, HNRPX, Alpha-CP1, Heterogeneous nuclear ribonucleoprotein E1, Nucleic acid-binding protein SUB2.3, PCBP1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDAGVTE SGLNVTLTIR LLMHGKEVGS IIGKKGESVK RIREESGARI NISEGNCPER IITLTGPTNA IFKAFAMIID KLEEDINSSM TNSTAASRPP VTLRLVVPAT QCGSLIGKGG CKIKEIREST GAQVQVAGDM LPNSTERAIT IAGVPQSVTE CVKQIC.
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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Name :
FABP3 Human, HisDescription:
Fatty Acid Binding Protein 3 Human Recombinant, His Tag
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
Product # :
PRO-668Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
FABP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 19.1 kDa. FABP3 is fused to a 37 amino acid His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
FABP3 His-Tag is supplied in 20mM Tris-HCl pH 8.0 and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Recombinant Fatty Acid Binding Protein is a newly introduced plasma marker of acute myocardial infarction (AMI). The plasma kinetics of FABP (15kD) closely resemble those of myoglobin in that elevated plasma concentrations are found within 2 hours after AMI and return to normal generally within 18 to 24 hours. But the concentration of FABP in the skeletal muscle is 20 times lower than in cardiac tissue (for myoglobin the same content for cardiac and skeletal tissue), that makes FABP to be more cardiac specific than myoglobin. This makes FABP a useful biochemical marker for the early assessment or exclusion of AMI. FABP also appears to be a useful plasma marker for the estimation of myocardial infarct size.
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Synonyms
Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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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.Please avoid freeze thaw cycles.
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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Name :
PBLD HumanDescription:
Phenazine Biosynthesis-Like Protein Domain Containing Human Recombinant
Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.
Product # :
PRO-010Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PBLD 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 308 amino acids (1-288 a.a.) and having a molecular mass of 33.9kDa. The PBLD is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PBLD solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
PBLD is member of the phenazine biosynthesis-like protein (PhzF) family. PBLD which is expressed in most tissues is the only representative of the PhzF family in the human genome. PBLD participates in the MAPK signaling pathway. PBLD is involved in multiple basic cellular functions, its expression is elevated in several disease processes, including folate deficiency and hypotension.
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Synonyms
Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MKLPIFIADA FTARAFRGNP AAVCLLENEL DEDMHQKIAR EMNLSETAFI RKLHPTDNFA QSSCFGLRWF TPASEVPLCG HATLASAAVL FHKIKNMNST LTFVTLSGEL RARRAEDGIV LDLPLYPAHP QDFHEVEDLI KTAIGNTLVQ DICYSPDTQK LLVRLSDVYN RSFLENLKVN TENLLQVENT GKVKGLILTL KGEPGGQTQA FDFYSRYFAP WVGVAEDPVT GSAHAVLSSY WSQHLGKKEM HAFQCSHRGG ELGISLRPDG RVDIRGGAAV VLEGTLTA.
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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Name :
PTPRN HumanDescription:
Protein Tyrosine Phosphatase Receptor Type N Human Recombinant
Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.
Product # :
ENZ-1162Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Human Protein Tyrosine Phosphatase Receptor Type N produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. PTPRN is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.
Source
Sf9 insect cells.
Formulation
PTPRN is supplied in 50mM Sodium phosphate (pH 8.0) and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein Tyrosine Phosphatase Receptor Type N (PTPRN) is a catalytically inactive protein and a major target of autoimmune response in diabetes mellitus. The long C-terminal intracellular tail covers the majority of autoantibody epitopes. PTPRN is expressed in neural, neuroendocrine and pancreatic islet cells.
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Synonyms
Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.
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Physical Appearance
Sterile Filtered colorless solution.
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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. Avoid multiple freeze-thaw cycles.
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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Name :
SPARC HumanDescription:
Secreted Protein Acidic & Rich in Cysteine Recombinant Human
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
Product # :
PRO-2602Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Secreted Protein Acidic & Rich in Cysteine Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 32.7kDa.SPARC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells is < 3.0 µg/mL, corresponding to a specific activity of > 333 IU/mg.
More Info
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Introduction
SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.
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Synonyms
Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SPARC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secreted Protein Acidic & Rich in Cysteine should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized SPARC in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI.
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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Name :
Protein A, 434 a.aDescription:
Staphylococcal Protein A 434 a.a Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-686Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Staphylococcal Protein A produced in E.Coli is a non-glycosylated, Polypeptide chain containing 434 amino acids (37-469 a.a.) and having a molecular mass of 48.1 kDa. Recombinant Staphylococcal Protein A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Protein-A protein solution contains 20mM Tris-HCl, pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MAQHDEAQQN AFYQVLNMPN LNADQRNGFI QSLKDDPSQS ANVLGEAQKL NDSQAPKADA QQNNFNKDQQ SAFYEILNMP NLNEAQRNGFIQSLKDDPSQ STNVLGEAKK LNESQAPKAD NNFNKEQQNA FYEILNMPNL NEEQRNGFIQ SLKDDPSQSA NLLSEAKKLN ESQAPKADNK
FNKEQQNAFY EILHLPNLNE EQRNGFIQSL KDDPSQSANL LAEAKKLNDA QAPKADNKFN KEQQNAFYEI LHLPNLTEEQ RNGFIQSLKDDPSVSKEILA EAKKLNDAQA PKEEDNNKPG KEDNNKPGKE DNNKPGKEDG NKPGKEDNKK PGKEDNKKPG KEDNKKPGKE DGNKPGKEDN
KKPGKEDGNG VHVVKPGDTV NDIAKANGTT ADKIAADNKL ADKNMIKPGQ ELVVDKKQPA NHADANKAQA LPET.
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.
- View Data Sheet
Name :
GrpE E.ColiDescription:
HSP-70 Cofactor (HSP24) E.Coli Recombinant
HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.
Product # :
HSP-014Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
GrpE Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids and having a molecular mass of 21.8 kDa. The GrpE is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The HSP24 protein solution contains 20mM Tris-HCl pH-8 and 0.1M NaCl.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
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Synonyms
HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKIANLEAQ LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA.
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.
- View Data Sheet
Name :
RBM11 HumanDescription:
RNA Binding Motif Protein 11 Human Recombinant
Splicing regulator RBM11, RNA-binding motif protein 11, RBM11.
Product # :
PRO-1802Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
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- purity
- More Info
Description
RBM11 Human Recombinant produced in E. coli is a single polypeptide chain containing 304 amino acids (1-281) and having a molecular mass of 34.6kDa. RBM11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RBM11 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
RNA Binding Motif Protein 11 (RBM11) which contains 1 RNA recognition motif is a part of the RBM family. The RBM gene family encodes proteins with an RNA binding motif which participate in the modulation of apoptosis. RBM11 is expressed in testis, kidney, spleen, brain, spinal cord and mammary gland and can be found as 2 isoforms produced by alternative splicing.
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Synonyms
Splicing regulator RBM11, RNA-binding motif protein 11, RBM11.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMFPAQEE ADRTVFVGNL EARVREEILY ELFLQAGPLT KVTICKDREG KPKSFGFVCF KHPESVSYAI ALLNGIRLYG RPINVQYRFG SSRSSEPANQ SFESCVKINS HNYRNEEMLV GRSSFPMQYF PINNTSLPQE YFLFQKMQWH VYNPVLQLPY YEMTAPLPNS ASVSSSLNHV PDLEAGPSSY KWTHQQPSDS DLYQMTAPLP NSASVSSSLN HVPDLEAGPS SYKWTHQQPS DSDLYQMNKR KRQKQTSDSD SSTDNNRGNE CSQKFRKSKK KKRY.
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.
- View Data Sheet
Name :
BMP3 HumanDescription:
Bone Morphogenetic protein-3 Human Recombinant
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
Product # :
CYT-937Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.More Info
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Introduction
Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.
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Synonyms
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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.
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Solubility
It is recommended to reconstitute the lyophilized BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
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Background
Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration
Abstract:
Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.
Production of BMP-3 Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.
Potential Therapeutic Applications:
BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.
Conclusion:
BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.
What is the molecular weight/Mw of BMP3 Protein?
BMP3 Protein has a total Mw of 24.8kDa.
What is the source or expression system of BMP3 Protein?
Escherichia Coli.
What is the Purity of BMP3 Protein?
BMP3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP3 Protein?
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.
What is the amino acid sequence of BMP3 Protein?
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
What applications can BMP3 Protein be used in?
BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP3 Protein?
The endotoxin level is minimal, BMP3 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.
- View Data Sheet
Name :
C5a HumanDescription:
Complement Component C5a Human Recombinant
Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.
Product # :
PRO-2300Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
- More Info
Description
C5a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8.3kDa.The Human C5a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Human C5a was lyophilized from a concentrated (1mg/ml) solution in PBS, pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml.More Info
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Introduction
Complement Component C5a (C5a) is involved in the complement system and it is encoded by the C5 gene in human. Complement C5 is cleaved into C5a and C5b. C5a has an imperative role in chemotaxis and C5b forms the 1st part of the complement membrane attack complex. Complement C5 is the 5th component of complement, which plays a central role in inflammatory and cell killing processes. C5a protein is composed of alpha and beta polypeptide chains, which are linked by a disulfide bridge. An activation peptide, C5a, which is an anaphylatoxin, which has potent spasmogenic and chemotactic activity, is derivative from the alpha polypeptide via cleavage with a convertase. The C5b macromolecular cleavage product forms a complex with the C6 complement component, and this complex is the basis for creation of the membrane attack complex, which includes supplementary complement components.
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Synonyms
Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Human C5a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human C5a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized C5a Human in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
TLQKKIEEIA AKYKHSVVKK CCYDGACVNN DETCEQRAAR ISLGPRCIKA FTECCVVASQ LRANISHKDM QLGR.
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.
- View Data Sheet
Name :
ATF HumanDescription:
Apo Transferrin Human
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-325Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
Human Apo Transferrin is a glycoprotein of approximately 77 kDa.
Source
Human serum.
Formulation
The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.
Purity
Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.
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Iron Content
The Iron content was estimated by ICP and was found to be <6 ppm.
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.
- View Data Sheet
Name :
FABP12 HumanDescription:
Fatty Acid Binding Protein-12 Human Recombinant
Fatty acid-binding protein 12, FABP12.
Product # :
PRO-738Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
FABP12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-140 a.a) and having a molecular mass of 18kDa.FABP12 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
FABP12 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
FABP12 is a member of the calycin superfamily and fatty-acid binding protein (FABP) family. The FABPs are a family of carrier proteins for fatty acids and other lipophilic substances for example eicosanoids and retinoids. These proteins are believed to enable the transfer of fatty acids between extra- and intracellular membranes. FABP12 has a role in lipid transport. FABP12 is expressed in several retinoblastoma cell lines. FABP12 has not been detected in fetal tissues.
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Synonyms
Fatty acid-binding protein 12, FABP12.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMIDQLQ GTWKSISCEN SEDYMKELGI GRASRKLGRL AKPTVTISTD GDVITIKTKS IFKNNEISFK LGEEFEEITP GGHKTKSKVT LDKESLIQVQ DWDGKETTIT RKLVDGKMVV ESTVNSVICT RTYEKVSSNS VSNS.
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.
- View Data Sheet
Name :
BLyS Human, PlantDescription:
BAFF (BLyS) Human Recombinant, Plant
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
Product # :
CYT-054Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
BAFF human Recombinant produced in Nicotiana benthamiana plant is a single glycosilated polypeptide chain containing 151 amino acids fragment (134-285).BAFF (C830H1277N223O242S5) is fused to a 10-His-tag at the N-terminal having the total molecular mass of 18-20kDa and purified by standard chromatographic techniques.
Source
Nicotiana benthamiana plant
Formulation
Lyophilized from 1mg/ml solution in 20 mM PBS buffer pH 7 and 0.2 M NaCl.
Purity
Greater than 97.0% as determined by Analysis by SDS-PAGE.
Biological Activity
The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
*activity results may vary with PBMC donors.
ED50 ? 50ng/mlMore Info
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Introduction
BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity.A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin. -
Synonyms
BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF 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.
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Solubility
It is recommended to reconstitute the lyophilized BAFF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL
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Background
What is the molecular weight/Mw of BLYS Protein?
BLYS Protein has a total Mw of 19kDa.
What is the source or expression system of BLYS Protein?
Escherichia Coli.
What is the Purity of BLYS Protein?
BLYS Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BLYS Protein?
The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
What is the amino acid sequence of BLYS Protein?
HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL
What applications can BLYS Protein be used in?
BLYS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BLYS Protein?
The endotoxin level is minimal, BLYS 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.
- View Data Sheet
Name :
CRKL HumanDescription:
V-crk Sarcoma Virus CT10 Oncogene Homolog (Avian)-Like Human Recombinant
Crk-like protein, CRKL.
Product # :
PRO-063Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- More Info
Description
CRKL 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 323 amino acids (1-303 a.a.) and having a molecular mass of 35.9kDa (Molecular size on SDS-PAGE will appear higher). The CRKL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRKL solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Crk-like protein (CRKL) is a protein kinase containing SH2 and SH3 (src homology) domains which activates the RAS and JUN kinase signaling pathways and transforms fibroblasts in a RAS-dependent manner. CRKL is a substitute of the BCR-ABL tyrosine kinase, it also has a role in fibroblast transformation by BCR-ABL, and has oncogenic potential.
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Synonyms
Crk-like protein, CRKL.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRDSSTCPGDYVL SVSENSRVSH YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPM GSVSAPNLPT AEDNLEYVRT LYDFPGNDAE DLPFKKGEIL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPAVS GSPGAAITPL PSTQNGPVFA KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD ENE.
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.
- View Data Sheet
Name :
FABP4 Human, HisDescription:
Fatty Acid Binding Protein 4 Human Recombinant, His Tag
Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.
Product # :
PRO-566Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- source
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Description
FABP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 18 kDa. FABP4 is fused to His tag at N-terminus and purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
FABP4 His-Tag is supplied in 20mM Tris HCL pH=8, 0.5mM DTT and 50% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Adipocyte fatty acid binding protein FABP4 is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells.
In mice, targeted mutations in FABP4 provide significant protection from hyperinsulinemia and insulin resistance in the context of both dietary and genetic obesity. Adipocytes obtained from FABP4-deficient mice also have reduced efficiency of ipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated FABP4 expression in macrophages upon differentiation and activation. In these cells, FABP4 modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific FABP4 deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for FABP4 in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages. -
Synonyms
Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.
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Physical Appearance
Sterile Filtered colorless liquid formulation.
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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.Please avoid freeze thaw cycles.
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.
- View Data Sheet
Name :
CSNK2B ProteinDescription:
Casein Kinase 2b Human Recombinant
Casein kinase II subunit beta, CK II beta, Phosvitin, G5a, CK2B, CK2N, CSK2B, MGC138222, MGC138224.
Product # :
PKA-223Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
CSNK2B Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 215 amino acids and having a total molecular mass of 24.9kDa. CK2 beta is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CSNK2B protein (1 mg/ml) contains 20mM Tris-HCl pH 8.0, 200mM NaCl, 1mM DTT, 1mM EDTA, 1uM leupeptin and 40% glycerol.
Purity
Greater than 95.0% as determinedAnalysis by SDS-PAGE.
More Info
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Introduction
Casein Kinase 2 also called CK2 (also called PKCK2) is a ubiquitous Ser/Thr kinase expressed in all eukaryotes. CK2 is a tetramer composed of two catalytic kinase domains, alpha subunits, and two identical regulatory beta subunits. It has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm, and other cellular processes. The beta subunit itself does not have kinase activity, but confers stability to the CK2 alpha subunit and is involved in activity and substrate specificity.
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Synonyms
Casein kinase II subunit beta, CK II beta, Phosvitin, G5a, CK2B, CK2N, CSK2B, MGC138222, MGC138224.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML
PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR.
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.
- View Data Sheet
Name :
Prelamin-ADescription:
Prelamin-A Recombinant
Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
Product # :
PRO-689Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Prelamin-A is a 74kDa precursor of the nuclear lamin A protein. Prelamin-A is a structural component of the nuclear lamina and it is encoded by lamin A/C gene (LMNA). Due to the presence of a CAAX box sequence at carboxyl terminus, Prelamin-A in vivo goes through a serial of post-translational modifications, resulting in the farnesylation of the cysteine thiol, removal of the AAX tripeptide, carboxyl-methylation of the cysteinyl carboxy group and proteolysis of 18 C-terminal amino acids residues that lead to mature lamin A. Diverse mutations in the lamin A/C gene are associated with different deseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. Recombinant human prelamin A is fused to a 6 Histidine tag at the N-terminus.
Source
Escherichia Coli.
Formulation
The Prelamin-A solution (0.1mg/ml) contains 10% Glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYL
LGNSSPRTQSPQNCSIM
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.
- View Data Sheet
Name :
MAPT Human 383a.a.Description:
Microtubule-Associated Protein Tau 383 a.a. Human Recombinant
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
Product # :
PRO-012Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MAPT Human Recombinant (Isoform 3) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 403 amino acids (1-383 a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
MAPT is a neuronal microtubule associated protein localized mostly on axons.
MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain. -
Synonyms
Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.
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Physical Appearance
Sterile Filtered colorless solution.
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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 prevent freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL.
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.