Search results
1000 results found for “cysteine-rich”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
CALM2 HumanDescription:
Calmodulin-2 Human Recombinant
PHKD, CAMII, PHKD2, Calmodulin-2, CALM2, CALM1 protein, Phosphorylase kinase delta.
Product # :
PRO-618Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant CALM2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 149 amino acids and having a molecular mass of 16 kDa. CALM2 is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The CALM2 solution (1mg/ml) contains 20mM Tris-HCl, pH-7.5.
Purity
Greater than 90.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Calmodulin-2 acts as an intracellular calcium sensor protein. When the intracellular Ca2+ concentration increases, calmodulin can bind up to four Ca2+, changing its conformation and regulating cellular functions such as activation or inhibition of a large number of enzymes, ion channels, and receptors. P53 protein stimulates CALM2 gene expression in 041 cells. CALM-2 is involved in the processes of Ca(2+)-induced neuronal cell death and the blockage of calmodulin attenuates brain injury after cerebral ischemia. Calmodulin-2 mediates the control of a large number of enzymes and other proteins by ca(2+). among the enzymes to be stimulated by the calmodulin-ca(2+) complex are a number of protein kinases and phosphatases.
-
Synonyms
PHKD, CAMII, PHKD2, Calmodulin-2, CALM2, CALM1 protein, Phosphorylase kinase delta.
-
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
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK.
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 :
CAPZA2 HumanDescription:
Capping Protein (Actin Filament) Muscle Z-Line Alpha 2 Human Recombinant
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
Product # :
PRO-1721Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CAPZA2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 309 amino acids (1-286 a.a) and having a molecular mass of 35.3kDa.CAPZA2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CAPZA2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, and 0.4M UREA.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2 also known as CAPZA2 belongs the F-actin capping protein alpha subunit family. It is the alpha subunit of the barbed-end actin binding protein Cap Z. By capping the barbed end of actin filaments, Cap Z regulates the growth of the actin filaments at the barbed end. Among the diseases associated with CAPZA2 are endocarditis, and cervicitis.
-
Synonyms
Capping Protein (Actin Filament) Muscle Z-Line, Alpha 2, F-Actin Capping Protein Alpha-2 Subunit, CapZ Alpha-2, CAPPA, CAPZ2, F-Actin-Capping Protein Subunit Alpha-2.
-
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 MGSMADLEEQ LSDEEKVRIA AKFIIHAPPG EFNEVFNDVR LLLNNDNLLR EGAAHAFAQY NLDQFTPVKI EGYEDQVLIT EHGDLGNGKF LDPKNRICFK FDHLRKEATD PRPCEVENAV ESWRTSVETA LRAYVKEHYP NGVCTVYGKK IDGQQTIIAC IESHQFQAKN FWNGRWRSEW KFTITPSTTQ VVGILKIQVH YYEDGNVQLV SHKDIQDSLT VSNEVQTAKE FIKIVEAAEN EYQTAISENY QTMSDTTFKA LRRQLPVTRT KIDWNKILSY KIGKEMQNA.
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 :
FIMC E.ColiDescription:
Chaperone Protein fimC E.Coli Recombinant
Chaperone protein fimC, fimC, b4316, JW4279.
Product # :
PRO-120Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
FIMC E.Coli Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 226 amino acids (37-241 a.a.) and having a molecular mass of 25kDa. The FIMC is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FIMC solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
The 23kDa two-domain periplasmic chaperone FIMC from E.coli is vital for the assembly of type-1 pili, which are filamentous, very oligomeric protein complexes anchored to the outer bacterial membrane that mediate adhesion of pathogenic E. coli strains to host cell surfaces and persist in macrophages.
-
Synonyms
Chaperone protein fimC, fimC, b4316, JW4279.
-
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 MGVALGATRV IYPAGQKQEQ LAVTNNDENS TYLIQSWVEN ADGVKDGRFI VTPPLFAMKG KKENTLRILD ATNNQLPQDR ESLFWMNVKA IPSMDKSKLT ENTLQLAIIS RIKLYYRPAK LALPPDQAAE KLRFRRSANS LTLINPTPYY LTVTELNAGT RVLENALVPP MGESTVKLPS DAGSNITYRT INDYGALTPK MTGVME.
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 :
PIN4 HumanDescription:
Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 4 Human Recombinant
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.
Product # :
ENZ-106Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
PIN4 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids (1-156 a.a.) and having a molecular mass of 18.8kDa.PIN4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PIN4 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 300 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-HCl pH8.0 using chymotrypsin.More Info
-
Introduction
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4 (PIN4) is a peptidyl-prolyl cis/trans isomerase (PPIase) which interacts with NIMA and is vital for cell cycle regulation. PIN4 has 2 different isoforms: PAR14 and PAR17. Furthermore, Pin4 protein binds to double-stranded DNA under physiological salt conditions.
-
Synonyms
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 4, Parvulin-14, Par14, hPar14, Parvulin-17, Par17, hPar17, Peptidyl-prolyl cis-trans isomerase Pin4, PPIase Pin4, Peptidyl-prolyl cis/trans isomerase EPVH, hEPVH, Rotamase Pin4, PIN4, EPVH, MGC138486.
-
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 MPMAGLLKGL VRQLERFSVQ QQASKMPPKG KSGSGKAGKG GAASGSDSAD KKAQGPKGGG NAVKVRHILC EKHGKIMEAM EKLKSGMRFN EVAAQYSEDK ARQGGDLGWM TRGSMVGPFQ EAAFALPVSG MDKPVFTDPP VKTKFGYHII MVEGRK.
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 :
TK1 HumanDescription:
Thymidine Kinase 1 Human Recombinant
Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.
Product # :
PKA-036Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TK1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.
-
Synonyms
Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.
-
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 MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.
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
Description:
Adiponectin Globular Recombinant, His Tag
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
Product # :
CYT-277Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Acrp30 Human has a total of 171 amino acids. N-terminal underlined amino acids are His-tag and the protease cleavage site (31AA-Underlined). The AA sequence of Acrp30 Human is homologous to the 105-244 amino acid sequence of the Human full-length Adiponectin (Swiss-prot entry Q15848).
Source
Escherichia Coli.
Formulation
Acrp30 Human is a filtered powder, lyophilized from 0.6mg/ml in PBS buffer.
Purity
Purity of Acrp30 Human is greater than 95% as determined by SDS PAGE.
More Info
-
Introduction
Adiponectin is a protein exclusively secreted from adipose tissue. In the circulation, adiponectin is present as three different oligomeric complexes, including the high molecular weight (HMW), the middle molecular weight (MMW, also called hexamer) and low molecular weigh (LMW, also called trimer) forms. Different oligomeric complex of adiponectin activates different signaling pathways and exerts distinct functions.
-
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
-
Stability
For long term, store lyophilized Acrp30 Human at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted Acrp30 Human can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C. The lyophilized Acrp30 Human remains stable for 24 months when stored at -20°C.
-
Solubility
Add deionized water and let the lyophilized pellet of Acrp30 Human dissolve completely.
-
Amino Acid Sequence
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.
-
Background
What is the molecular weight/Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 16.7kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.
What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ADIPONECTIN Protein?
The biological functionality of ADIPONECTIN Protein will be determined in the future.
What is the amino acid sequence of ADIPONECTIN Protein?
MSWWHHHHHH NWNIPTTQDT TQDLWFEGAM GGEGAYVYRS FSVGLETYV TIPNMPIRFT KIFYNQQNHYDGSTGKFHCN IPGLYYFAYH ITVYMKDVKV SLFKKDKAML FTYDQYQENN VDQASGSVLL HEVGDQVWLQVYGEGERNGL YADNDNDSTF TGFLLYHDTN.
What applications can ADIPONECTIN Protein be used in?
ADIPONECTIN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ADIPONECTIN Protein?
The endotoxin level is minimal, ADIPONECTIN 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 :
CDKN1B HumanDescription:
Cyclin-Dependent Kinase Inhibitor 1B Human Recombinant
Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1, CDKN1B, KIP1, MEN4, CDKN4, MEN1B.
Product # :
PKA-012Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CDKN1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 218 amino acids (1-198 a.a.) and having a molecular mass of 24.2kDa (Molecular weight on SDS-PAGE will appear higher).CDKN1B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CDKN1B protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cyclin-dependent kinase inhibitor 1B (CDKN1B) is a member of the Cip/Kip family of cyclin dependent kinase (Cdk) inhibitor proteins. The CDKN1B protein binds to and prevents the activation of cyclin E-CDK2 or cyclin D-CDK4 complexes, and so controls the cell cycle progression at G1. CDKN1B is often referred to as a cell cycle inhibitor protein since its major function is to stop or slow down the cell division cycle. The degradation of the CDKN1B protein, which is triggered by its CDK dependent phosphorylation and ensuing ubiquitination by SCF complexes, is compulsory for the cellular transition from inactive to the proliferative state.
-
Synonyms
Cyclin-dependent kinase inhibitor 1B, Cyclin-dependent kinase inhibitor p27, p27Kip1, CDKN1B, KIP1, MEN4, CDKN4, MEN1B.
-
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 MSNVRVSNGS PSLERMDARQ AEHPKPSACR NLFGPVDHEE LTRDLEKHCR DMEEASQRKW NFDFQNHKPL EGKYEWQEVE KGSLPEFYYR PPRPPKGACK VPAQESQDVS GSRPAAPLIG APANSEDTHL VDPKTDPSDS QTGLAEQCAG IRKRPATDDS STQNKRANRT EENVSDGSPN AGSVEQTPKK PGLRRRQT.
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 :
PROSC HumanDescription:
Proline Synthetase Co-Transcribed Human Recombinant
Proline Synthetase Co-Transcribed Homolog (Bacterial), Proline Synthetase Co-Transcribed (Bacterial Homolog), Proline Synthase Co-Transcribed Bacterial Homolog Protein, Proline Synthetase Co-Transcribed Bacterial Homolog Protein, PROSC.
Product # :
PRO-481Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PROSC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275) and having a molecular mass of 32.7 kDa.PROSC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PROSC solution (0.5mg/ml) contains 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.
More Info
-
Introduction
Proline Synthetase Co-Transcribed (PROSC) is a member of the UPF0001 family.
-
Synonyms
Proline Synthetase Co-Transcribed Homolog (Bacterial), Proline Synthetase Co-Transcribed (Bacterial Homolog), Proline Synthase Co-Transcribed Bacterial Homolog Protein, Proline Synthetase Co-Transcribed Bacterial Homolog Protein, PROSC.
-
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 MGSMWRAGSM SAELGVGCAL RAVNERVQQA VARRPRDLPA IQPRLVAVSK TKPADMVIEA YGHGQRTFGE NYVQELLEKA SNPKILSLCP EIKWHFIGHL QKQNVNKLMA VPNLFMLETV DSVKLADKVN SSWQRKGSPE RLKVMVQINT SGEESKHGLP PSETIAIVEH INAKCPNLEF VGLMTIGSFG HDLSQGPNPD FQLLLSLREE LCKKLNIPAD QVELSMGMSA DFQHAVEVGS TNVRIGSTIF GERDYSKKPT PDKCAADVKA PLEVAQEH.
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 :
CXCL2 RatDescription:
GRO-beta/MIP-2 Rat Recombinant (CXCL2)
Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta, CINC-3.
Product # :
CHM-372Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GRO-Beta Rat Recombinant also called Rat MIP-2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7923 Dalton. The GRO-b 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 99.0% as determined by SDS-PAGE.
Biological Activity
The biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.More Info
-
Introduction
Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.
-
Synonyms
Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta, CINC-3.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GRO-b although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Rat in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.
-
Background
What is the molecular weight/Mw of CXCL2 RAT Protein?
CXCL2 RAT Protein has a total Mw of 7.92kDa.
What is the source or expression system of CXCL2 RAT Protein?
Escherichia Coli.
What is the Purity of CXCL2 RAT Protein?
CXCL2 RAT Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL2 RAT Protein?
The biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 100,000-1,000,000 units/mg.
What is the amino acid sequence of CXCL2 RAT Protein?
VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.
What applications can CXCL2 RAT Protein be used in?
CXCL2 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL2 RAT Protein?
The endotoxin level is minimal, CXCL2 RAT 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 :
GroES E.ColiDescription:
GroES (HSP10) E.Coli Recombinant
CPN10, GROES, HSP10, HSPE1, 10 kDa chaperonin, Protein Cpn10, groES protein, 11.2 kDa stress response protein, Heat shock protein 10.
Product # :
HSP-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant GroES produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 10.4 kDa.
Source
Escherichia Coli.
Formulation
The GroES protein (1mg/ml) contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
-
Introduction
GroES protein is the co-chaperonin of GroES in E.coli and assists protein folding. GroEL mediated folding requires the co-chaperonin GroES which is essential for viability. GroES is composed of a single heptameric ring of 10kDa subunits that binds to the ends of the GroEL cylinder. GroES gene was amplified by PCR from E.coli and cloned into an expression vector. This protein was overexpressed in E.coli and was purified by using conventional chromatography techniques.
-
Synonyms
CPN10, GROES, HSP10, HSPE1, 10 kDa chaperonin, Protein Cpn10, groES protein, 11.2 kDa stress response protein, Heat shock protein 10.
-
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
MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE GEVKPLDVKVGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA.
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 :
UROD HumanDescription:
Uroporphyrinogen Decarboxylase Human Recombinant
UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.
Product # :
ENZ-536Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
UROD Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 43 kDa. The UROD is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UROD Human solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl, 1mM EDTA & 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
UROD is the fifth enzyme in the human heme biosynthetic pathway and is in charge for the transfer of uroporphyrinogen to coproporphyrinogen through the deletion of four carboxymethyl side chains. UROD Mutations and deficiency result in 3 autosomal disorders in humans: familial porphyria cutanea tarda (f-PCT), sporadic porphyria cutanea tarda (s-PCT) and hepatoerythropoietic porphyria (HEP).
-
Synonyms
UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.
-
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 MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT LQVNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH SRLLRQN.
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 :
Troponin-C ProteinDescription:
Cardiac Troponin-C Human
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
Product # :
PRO-2571Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Troponin-C Human produced from Human Cardiac Tissue, having a molecular mass of 18kDa. The Troponin-C is purified using a combination of ion-exchange and affinity chromatography steps.
Source
Human cardiac tissue
Formulation
The protein solution contains 150 mM NaCl, 10 mM sodium phosphate and 0.05% NaN3, (pH 7.0).
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Troponin is a fundamental regulatory protein of striated muscle contraction, and together with tropomyosin, is positioned on the actin filament. Troponin has 3 subunits: TnI- the inhibitor of actomyosin ATPase; TnT- contains the binding site for tropomyosin; and TnC- the protein encoded by the TNNC1 gene. The binding of calcium to TnC stops the inhibitory action of TnI, consequently allowing the interaction of actin with myosin, the hydrolysis of ATP, and the generation of tension. Mutations in the TNNC1 gene are linked to cardiomyopathy dilated type 1Z.
-
Synonyms
Troponin C slow skeletal and cardiac muscles, TN-C, TNNC1, TNNC, TNC, CMD1Z.
-
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.
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 :
GOT1 MouseDescription:
Glutamic-Oxaloacetic Transaminase 1 Mouse Recombinant
Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.
Product # :
ENZ-872Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GOT1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 436 amino acids (1-413a.a) and having a molecular mass of 48.6kDa.GOT1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GOT1 protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GOT1 is a pyridoxal phosphate-dependent enzyme which exists in cytoplasmic and mitochondrial forms, GOT1 and GOT2, which participate in amino acid metabolism and the urea and tricarboxylic acid cycles. Both enzymes are homodimeric and show close homology.
-
Synonyms
Aspartate aminotransferase, cytoplasmic, cAspAT, Cysteine aminotransferase, cytoplasmic, Cysteine transaminase, cytoplasmic, cCAT, Glutamate oxaloacetate transaminase 1, Transaminase A.
-
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 MGSMAPPSVF AQVPQAPPVL VFKLTADFRD DPDPRKVNLG VGAYRTDESQ PWVLPVVRKV EQKIANDNSL NHEYLPILGL AEFRSCASRL VLGDNSPAIR ENRVGGVQSL GGTGALRIGA DFLGRWYNGT DNKNTPIYVS SPTWENHNAV FSAAGFKDIR PYCYWDAEKR GLDLQGFLND LENAPEFSIF VLHACAHNPT GTDPTPEQWK QIAAVMQRRF LFPFFDSAYQ GFASGDLEKD AWAIRYFVSE GFELFCAQSF SKNFGLYNER VGNLTVVGKE SDSVLRVLSQ MEKIVRITWS NPPAQGARIV AATLSDPELF KEWKGNVKTM ADRILTMRSE LRARLEALKT PGTWSHITEQ IGMFSFTGLN PKQVEYLVNE KHIYLLPSGR INMCGLTTKN LDYVATSIHE AVTKIQ.
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 :
GDF15 Human, HisDescription:
Growth and Differentiation Factor 15 Human Recombinant, His Tag
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
Product # :
CYT-691Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
-
Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
-
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
-
Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.
What is the source or expression system of GDF15 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of GDF15 HUMAN, HIS Protein?
The biological functionality of GDF15 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
What applications can GDF15 HUMAN, HIS Protein be used in?
GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and
Lateral Flow.
What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 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.
- View Data Sheet
Name :
SERPINA4 HumanDescription:
Kallistatin Human Recombinant
Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin) Member 4, PI4, KST, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 4, Peptidase Inhibitor 4, Kallikrein Inhibitor, Serpin A4, PI-4, Protease Inhibitor 4 (Kallistatin), Kallistatin, KLST, KAL, SERPINA4.
Product # :
PRO-2036Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
SERPINA4 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (Gln21-Pro427) containing a total of 417 amino acids, having a calculated molecular mass of 47.7kDa and fused to a 10 aa His tag at C-Terminus.
Source
HEK 293.
Formulation
SERPINA4 was filtered (0.4µm) and lyophilized from 0.5mg/ml solution in phosphate buffered saline pH 7.4 and 5% (w/v) Trehalose.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Kallistatin (SERPINA4) inhibits human amidolytic and kininogenase activities of tissue kallikrein. This inhibition is attained by formation of an equimolar, heat- and SDS-stable complex between the inhibitor and the enzyme, and production of a small C-terminal fragment of the inhibitor as a result of cleavage at the reactive site by tissue kallikrein.
-
Synonyms
Serpin Peptidase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin) Member 4, PI4, KST, Serine (Or Cysteine) Proteinase Inhibitor, Clade A (Alpha-1 Antiproteinase, Antitrypsin), Member 4, Peptidase Inhibitor 4, Kallikrein Inhibitor, Serpin A4, PI-4, Protease Inhibitor 4 (Kallistatin), Kallistatin, KLST, KAL, SERPINA4.
-
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 two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. SERPINA4 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
QLHVEHDGES CSNSSHQQIL ETGEGSPSLK IAPANADFAF RFYYLIASET PGKNIFFSPL SISAAYAMLS LGACSHSRSQ ILEGLGFNLT ELSESDVHRG FQHLLHTLNL PGHGLETRVG SALFLSHNLK FLAKFLNDTM AVYEAKLFHT NFYDTVGTIQ LINDHVKKET RGKIVDLVSE LKKDVLMVLV NYIYFKALWE KPFISSRTTP KDFYVDENTT VRVPMMLQDQ EHHWYLHDRY LPCSVLRMDY KGDATVFFIL PNQGKMREIE EVLTPEMLMR WNNLLRKRNF YKKLELHLPK FSISGSYVLD QILPRLGFTD LFSKWADLSG ITKQQKLEAS KSFHKATLDV DEAGTEAAAA TSFAIKFFSA QTNRHILRFN RPFLVVIFST STQSVLFLGK VVDPTKPHHH HHHHHHH.
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 :
TROVE2 BovineDescription:
TROVE Domain Family, Member 2, Bovine
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
Product # :
PRO-111Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TROVE2 is a natural protein having a molecular mass of 60kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.
Source
Bovine tissues.
Formulation
TROVE2 is supplied in 20mM Tris/HCl buffer pH-7.5, 150mM NaCl, 2mM MgCl2, 0.2mM DTT, 0.1mM PMSF and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.
-
Synonyms
60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.
-
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.
-
Immunological Functions
1. Binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.
-
coating concentration
0.2-0.6 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.
-
Applications
Western blot with SLE sera (secondary Sjogren’s syndrome).
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 :
SIRPA Human, HEKDescription:
Signal-Regulatory Protein Alpha Human Recombinant, HEK
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptorSHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR.
Product # :
PRO-2755Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
SIRPA Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-373a.a) containing 356 amino acids and having a molecular mass of 39kDa.SIRPA is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The SIRPA solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human CD47.
More Info
-
Introduction
Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as the immunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which are involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.
SIRPA can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part in signal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA. -
Synonyms
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptor
SHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR. -
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
DGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY 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.
- View Data Sheet
Name :
CGB3 HumanDescription:
CGB3 Human Recombinant
CGB3 CGB5 CGB8, CGB5, CGB7, CGB8, HCGB, CG-beta.
Product # :
PRO-2398Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CGB3 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 154 amino acids (21-165.a.) and having a molecular mass of 16.6kDa (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). CGB3 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CGB3 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
CGB3, belongs to the glycoprotein hormone beta chain family. CGB3 encodes the beta 3 subunit. CGB3 stimulates the expression of GCM1 target genes, as well as the fusogenic protein syncytin-1, to promote placental cell fusion. Furthermore, CGB3 is synthesized in large quantities by the growing placenta, reaching peak concentrations in maternal blood throughout the late first trimester and early mid-trimester of pregnancy. CGB3 is expressed solely by trophoblasts. CGB3 is a significant biomarker in pregnancy and oncology, where it is routinely detected and quantified by specific immunoassays.
-
Synonyms
CGB3 CGB5 CGB8, CGB5, CGB7, CGB8, HCGB, CG-beta.
-
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
ADPSKEPLRP RCRPINATLA VEKEGCPVCI TVNTTICAGY CPTMTRVLQG VLPALPQVVC NYRDVRFESI RLPGCPRGVN PVVSYAVALS CQCALCRRST TDCGGPKDHP LTCDDPRFQD SSSSKAPPPS LPSPSRLPGP SDTPILPQHH 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.
- View Data Sheet
Name :
COX5B HumanDescription:
Cytochrome C Oxidase Subunit Vb Human Recombinant
Cytochrome c oxidase subunit 5B, mitochondrial precursor, COXVB, COX5B, Mitochondrial, Cytochrome c oxidase polypeptide Vb.
Product # :
PRO-1513Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
COX5B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 121 amino acids (32-129a.a) and having a molecular mass of 13kDa. COX5B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
COX5B protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cytochrome c oxidase subunit VB (COX5B) is the terminal enzyme of the mitochondrial respiratory chain. COX5B is a multi-subunit enzyme complex which couples the transfer of electrons from cytochrome c to molecular oxygen and contributes to a proton electrochemical gradient across the inner mitochondrial membrane. There are two isoforms of COX5:COX5a and COX5b. Transcription of COX5A (the aerobic isoform) is up-regulated as the rate of cellular respiration increases, when oxygen levels within the cell are high. However, when oxygen levels are low, COX5B (the hypoxic isoform) transcription increases and functions to maximize the turnover rate of the COX apoenzyme.
-
Synonyms
Cytochrome c oxidase subunit 5B, mitochondrial precursor, COXVB, COX5B, Mitochondrial, Cytochrome c oxidase polypeptide Vb.
-
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 MGSASGGGVP TDEEQATGLE REIMLAAKKG LDPYNVLAPK GASGTREDPN LVPSISNKRI VGCICEEDNT SVVWFWLHKG EAQRCPRCGA HYKLVPQQLA 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.
- View Data Sheet
Name :
ZWINT HumanDescription:
ZW10 Interacting Kinetochore Protein Human Recombinant
ZW10 Interacting Kinetochore Protein, ZWINT, ZW10 Interactor, HZwint-1, KNTC2AP, ZWINT1, Human ZW10 Interacting Protein-1, ZW10 Interactor Kinetochore Protein zwint-1, Zwint-1, ZW10-Interacting Protein 1.
Product # :
PRO-1944Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ZWINT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 253 amino acids (1-230) and having a molecular mass of 27.9 kDa (Molecular size on SDS-PAGE will appear higher).ZWINT is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ZWINT solution (0.25mg/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
-
Introduction
ZW10 Interacting Kinetochore Protein (ZWINT) is involved in kinetochore function. ZWINT is part of the MIS12 complex, which is essential for kinetochore formation and spindle checkpoint activity. ZWINT is localized to the cytoplasm during interphase and to kinetochores from late prophase to anaphase. ZWINT interacts with ZW10 (Zeste White 10) and regulates the association between ZW10 and kinetochores. ZWINT gene defects are linked with the pathogenesis of Roberts’s syndrome, an autosomal recessive disorder characterized by growth retardation due to premature chromosome separation.
-
Synonyms
ZW10 Interacting Kinetochore Protein, ZWINT, ZW10 Interactor, HZwint-1, KNTC2AP, ZWINT1, Human ZW10 Interacting Protein-1, ZW10 Interactor Kinetochore Protein zwint-1, Zwint-1, ZW10-Interacting Protein 1.
-
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 MGSMEAAETE AEAAALEVLA EVAGILEPVG LQEEAELPAK ILVEFVVDSQ KKDKLLCSQL QVADFLQNIL AQEDTAKGLD PLASEDTSRQ KAIAAKEQWK ELKATYREHV EAIKIGLTKA LTQMEEAQRK RTQLREAFEQ LQAKKQMAME KRRAVQNQWQ LQQEKHLQHL AEVSAEGKLL FPEAEAEAEN LPDDKPQQPT RPQEQSTGDT MGRDPGVSFK AVGLQPAGDV NLP.
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 :
GCVDescription:
Ganciclovir
Product # :
SYN-001Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- purity
- More Info
Description
Ganciclovir is a white to off-white crystalline powder with a molecular formula of C9H13N5O4 and a molecular weight of 255.23.
Purity
Greater than 99.0%.
More Info
-
Introduction
Ganciclovir (GCV) is a pro-drug nucleoside analog that is activated by phosphorylation. It is useful in the study of gene therapy in cancer research.
Ganciclovir is a synthetic analogue of 2'-deoxy-guanosine. It is initially phosphorylated to a deoxyguanosine triphosphate (dGTP) analogue. This mechanism competitively inhibits the integration of dGTP by viral DNA polymerase, resulting in the termination of elongation of viral DNA. Upon expression of a viral suicide gene encoding thymidine kinase, the non-toxic pro-drug is converted to a phosphorylated active analog and is incorporated into the DNA of replicating eukaryotic cells, causing death of the malignant dividing cell. The cell cycle is irreversibly arrested at the G2-M checkpoint. Gap junction involvement in the ganciclovir bystander effect has been studied. Ganciclovir has been used to study loss of telomeres and to evaluate sensitivity of viruses to antiviral treatments.
Ganciclovir is used in molecular biology for selection against random recombination events when homologous recombination of a gene of interest is required. -
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Ganciclovir although stable at room temperature for 3 weeks, should be stored at 4°C.
-
Solubility
It is recommended to reconstitute the lyophilized Ganciclovir in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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 :
CCL15 HumanDescription:
Macrophage Inflammatory Protein-5 Human Recombinant (CCL15)
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
Product # :
CHM-230Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Macrophage Inflammatory Protein-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 92 amino acids and having a molecular mass of 10.1 kDa. The MIP5 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIP5 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 100mM NaCl.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.More Info
-
Introduction
CCL15, a new human CC chemokine, was isolated from a human fetal spleen cDNA library. CCL15 cDNA encodes a predicted 113 amino acid (aa) protein containing a putative signal peptide of 21 amino acids that is cleaved to generate a 92 aa residue mature protein. Within the CC family members, human CCL15 shares 45%, 44%, 35%, and 30% aa homology with mouse C10, human MPIF-1, human HCC-1, and mouse MIP-1?, respectively. The gene for MIP-5 is found on chromosome 17 where the genes for most of the human CC chemokines are located. Human CCL15 is expressed in T and B lymphocytes, NK cells, monocytes and monocyte-derived dendritic cells. Human MIP-5 is chemotactic for T cells and monocytes and has been shown to induce calcium flux in human CCR-1-transfected cells.
-
Synonyms
Small inducible cytokine A15 precursor, CCL15, Macrophage inflammatory protein 5, MIP-5, MIP5, Chemokine CC-2, HCC-2, NCC-3, MIP- 1 delta, Leukotactin-1, LKN-1, Mrp-2b, C-C motif chemokine 15.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MIP-5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL15 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 MIP5 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.
-
Background
What is the molecular weight/Mw of CCL15 HUMAN Protein?
CCL15 HUMAN Protein has a total Mw of 10.1kDa.
What is the source or expression system of CCL15 HUMAN Protein?
Escherichia Coli.
What is the Purity of CCL15 HUMAN Protein?
CCL15 HUMAN Protein is > 97% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL15 HUMAN Protein?
Determined by its ability to chemoattract human T-lymphocytes using a concentration range of 1-10 ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.
What is the amino acid sequence of CCL15 HUMAN Protein?
QFINDAETELMMSKLPLENPVVLNSFHFAADCCTSYISQSIPCSLMKSYFETSSECSKP GVIFLTKKGRQVCAKPSGPGVQDCMKKLKPYSI.
What applications can CCL15 HUMAN Protein be used in?
CCL15 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL15 HUMAN Protein?
The endotoxin level is minimal, CCL15 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
DHH (C23II) HumanDescription:
Desert Hedgehog (C23II) Human Recombinant
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
Product # :
CYT-362Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
DHH (C23II) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids and having a molecular mass of 19.9kDa. The DHH (C23II) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The Biological Activity was determined by its ability to induce alkaline phosphatase production by C3H/10T1/2 (CCL-226) cells. The expected ED50 for this effect is 15-45 μg/ml.More Info
-
Introduction
DHH is part of the Hedgehog family which encodes signaling molecules that are involved in regulating morphogenesis. DHH protein is a precursor that is autocatalytically cleaved, the N-terminal portion is soluble and contains the signalling activity while the C-terminal portion is involved in precursor processing. Additionally, the C-terminal product covalently attaches a cholesterol moiety to the N-terminal product, restricting the N-terminal product to the cell surface and preventing it from freely diffusing throughout the organism. Defects in DHH protein have been associated with partial gonadal dysgenesis (PGD) accompanied by minifascicular polyneuropathy. DHH plays a role both male gonadal differentiation and perineurial development.
DHH plays a role in intercellular signaling which is essential for a variety of patterning events during development. DHH functions as a spermatocyte survival factor in the testes & is essential for testes development. -
Synonyms
HHG-3, Desert Hedgehog homolog, MGC35145, Desert hedgehog protein, DHH.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized DHH (C23II) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution DHH (C23II) 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 DHH (C23II) in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
IIGPGRGPVG RRRYARKQLV PLLYKQFVPG VPERTLGASG PAEGRVARGS ERFRDLVPNY NPDIIFKDEE NSGADRLMTE RCKERVNALA IAVMNMWPGV RLRVTEGWDE DGHHAQDSLH YEGRALDITT SDRDRNKYGL LARLAVEAGF DWVYYESRNH VHVSVKADNS LAVRAGG.
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 :
FGF4 HumanDescription:
Fibroblast Growth Factor-4 Human Recombinant
HBGF4, FGF-4, FGF4, KFGF, HSTF1.
Product # :
CYT-312Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa. The FGF4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FGF4 protein was lyophilized with 20mM sodium phosphate and 500mM NaCl pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.
More Info
-
Introduction
FGF4 holds s comprehensive mitogenic and cell survival activities and takes part in a range of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF4 possess oncogenic transforming activity. FGF4 and FGF3, oncogenic growth factors are localized on chromosome 11. Co-amplification of both factors was found in several kinds of human tumors. FGF4 functions in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway.
-
Synonyms
HBGF4, FGF-4, FGF4, KFGF, HSTF1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FGF4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-4 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized FGF4 Human Recombinant sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.
-
Background
What is the molecular weight/Mw of FGF4 HUMAN Protein?
FGF4 HUMAN Protein has a total Mw of 19.8kDa.
What is the source or expression system of FGF4 HUMAN Protein?
Escherichia Coli.
What is the Purity of FGF4 HUMAN Protein?
FGF4 HUMAN Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF4 HUMAN Protein?
The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.
What is the amino acid sequence of FGF4 HUMAN Protein?
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.
What applications can FGF4 HUMAN Protein be used in?
FGF4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF4 HUMAN Protein?
The endotoxin level is minimal, FGF4 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.