Search: 1000 results found for "retinoblastoma"

Description:

Ubiquitin Biotinylated Human Recombinant

Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.

Product # :

PRO-629

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

Recombinant Human RPS27A protein biotinylated with NHS-biotin produced in E.Coli is a single, non-glycosylated polypeptide chain containing a total of 76 amino acids and having a molecular mass of 8.6 kDa.

Source

Escherichia Coli.

Formulation

The RPS27A is supplied in 1x PBS and 0.05% PBS.

Purity

RPS27A Protein biotinilation is determined by Western Blotting and ELISA analysis using streptavidin–HRP conjugated as a detection reagent. Free biotin is eliminated by dialysis against PBS. Protein concentration is determined by 280nm absorbance.

More Info

Introduction
Recombinant Human Ubiquitin having the accession number of P62988 was conjugated to Biotin. RPS27A is a small protein composed of 76 amino acids. RPS27A is found only in eukaryotic organisms among which shows strong sequence conservation. The RPS27A protein is present in all cell types, thus giving rise to its name.
RPS27A is found either in free form or conjugated to proteins through a covalent bond between the glycine at the C-terminal end and the side chains of lysine.
The connection of multiple copies of RPS27A targets the proteins for degradation by the 26S proteosome. RPS27A ligation is an ATP-dependent multi-step process. RPS27A is activated by the E1 enzyme. The attachment of RPS27A to the target protein is catalyzed by the E2 enzyme acting in concert with E3 which is involved in the recognition of the substrate protein.
Synonyms
Ubiquitin, Ribosomal Protein S27a, CEP80, UBA80, UBCEP1, UBCEP80, HUBCEP80, RPS27A.
Physical Appearance
Sterile Filtered colorless liquid formulation.
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.

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

Description:

Neurotrophin-3 Human Recombinant

Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

Product # :

CYT-257

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from 0.1% TFA.

Purity

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

Biological Activity

The ED₅₀ as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.

More Info

Introduction
NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.
Synonyms
Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.
Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of NT-3 as a Reference Standard.

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

Description:

SCAN domain containing 1 Human Recombinant

RAZ1, SDP1, SCAN domain containing 1, SCAN-related protein RAZ1.

Product # :

PRO-269

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

SCAND1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-179 a.a.) and having a molecular mass of 21.2kDa (molecular weight on SDS-PAGE will appear higher).SCAND1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SCAND1 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0) 1mM DTT, 100mM NaCl and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
SCAND1 is a part of a family of genes which encode an isolated SCAN domain. SCAN domain containing 1 has one SCAN box domain and has no zinc finger motif, which distinct this protein from almost all other SCAN domain containing proteins. SCAND1 is a nuclear protein that takes a part in the mechanism of transcription regulation. SCAND1 is extensively expressed in high levels in the kidney, thyroid, liver, prostate and testis.
Synonyms
RAZ1, SDP1, SCAN domain containing 1, SCAN-related protein RAZ1.
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 MAATEPILAA TGSPAAVPPE KLEGAGSSSA PERNCVGSSL PEASPPAPEP SSPNAAVPEA IPTPRAAASA ALELPLGPAP VSVAPQAEAE ARSTPGPAGS RLGPETFRQR FRQFRYQDAA GPREAFRQLR ELSRQWLRPD IRTKEQIVEM LVQEQLLAIL PEAARARRIR RRTDVRITG

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

Description:

Vascular Endothelial Growth Factor Receptor-3 Human Recombinant

Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.

Product # :

PKA-244

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Soluble FLT4 Human Recombinant fused with a carboxy-terminal 6X histidine-tag produced in baculovirus is a monomeric, glycosylated, polypeptide containing the extracellular part, 25-774 amino acids and having a total molecular mass of 120 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding. The FLT4 is purified by proprietary chromatographic techniques.

Source

Insect Cells.

Formulation

FLT4 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

Measured by its ability to bind recombinant rat VEGF-C in a functional solid phase binding assay. Immobilised recombinant human VEGFR-3/FLT-4 at 5 µg/ml can bind recombinant rat VEGF-C in a linear range of 8-500 ng/ml.

More Info

Introduction
All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis.
Synonyms
Tyrosine-protein kinase receptor FLT4, PCL, FLT41, FMS-LIKE TYROSINE KINASE 4, VEGFR-3, VEGFR3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FLT4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FLT4 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 FLT4 in sterile water not less than 100 µg/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.

Description:

Tubulin Gamma 1 Human Recombinant, Sf9

Tubulin gamma-1 chain, Gamma-1-tubulin, Gamma-tubulin complex component 1, GCP-1, TUBG1, TUBG, Tubulin, Gamma 1, Gamma-1-Tubulin, TUBGCP1, CDCBM4.

Product # :

PRO-2532

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

TUBG1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 457 amino acids (1-451 a.a.) and having a molecular mass of 51.9kDa. TUBG1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Insect cells.

Formulation

TUBG1 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 8.0) containing 40% glycerol, 0.1M NaCl,2mM DTT and 50mM imidazole.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
TUBG1 belongs to the tubulin superfamily. TUBG1 localizes to the centrosome and binds to microtubules to create the gamma-tubulin ring complex. TUBG1 facilitates the microtubule nucleation and is essential for microtubule formation and progression of the cell cycle.
Synonyms
Tubulin gamma-1 chain, Gamma-1-tubulin, Gamma-tubulin complex component 1, GCP-1, TUBG1, TUBG, Tubulin, Gamma 1, Gamma-1-Tubulin, TUBGCP1, CDCBM4.
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
MPREIITLQL GQCGNQIGFE FWKQLCAEHG ISPEGIVEEF ATEGTDRKDV FFYQADDEHY IPRAVLLDLE PRVIHSILNS PYAKLYNPEN IYLSEHGGGA GNNWASGFSQ GEKIHEDIFD IIDREADGSD SLEGFVLCHS IAGGTGSGLG SYLLERLNDR YPKKLVQTYS VFPNQDEMSD VVVQPYNSLL TLKRLTQNAD CVVVLDNTAL NRIATDRLHI QNPSFSQINQ LVSTIMSAST TTLRYPGYMN NDLIGLIASL IPTPRLHFLM TGYTPLTTDQ SVASVRKTTV LDVMRRLLQP KNVMVSTGRD RQTNHCYIAI LNIIQGEVDP TQVHKSLQRI RERKLANFIP WGPASIQVAL SRKSPYLPSA HRVSGLMMAN HTSISSLFER TCRQYDKLRK REAFLEQFRK EDMFKDNFDE MDTSREIVQQ LIDEYHAATR PDYISWGTQE QHHHHHH.

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

Description:

Chromogranin B Human Recombinant

SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.

Product # :

PRO-824

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

CHGB Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 677 amino acids (21-677 a.a.) and having a molecular mass of 78.4kDa. CHGB protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

Source

Escherichia Coli.

Formulation

The CHGB protein 0.25mg/ml solution containing 20mM Tris-HCl pH-8, 0.15M NaCl & 10% glycerol.

Purity

Greater than 80% as determined by SDS-PAGE.

More Info

Introduction
CHGB is a neuroendocrine secretory granule protein, that is the precursor for other biologically active peptides. CHGB is part of the chromogranin/secretogranin protein family and is expressed in the adrenal medulla, and in pheochromocytoma.
Synonyms
SCG1, Secretogranin 1, secretogranin B, CHGB, Sgl, CgB.
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 MPVDNRNHNE GMVTRCIIEV LSNALSKSSA PPITPECRQV LKTSRKDVKD KETTENENTK FEVRLLRDPA DASEAHESSS RGEAGAPGEE DIQGPTKADT EKWAEGGGHS RERADEPQWS LYPSDSQVSE EVKTRHSEKS QREDEEEEEG ENYQKGERGE DSSEEKHLEE PGETQNAFLN ERKQASAIKK EELVARSETH AAGHSQEKTH SREKSSQESG EEAGSQENHP QESKGQPRSQ EESEEGEEDA TSEVDKRRTR PRHHHGRSRP DRSSQGGSLP SEEKGHPQEE SEESNVSMAS LGEKRDHHST HYRASEEEPE YGEEIKGYPG VQAPEDLEWE RYRGRGSEEY RAPRPQSEES WDEEDKRNYP SLELDKMAHG YGEESEEERG LEPGKGRHHR GRGGEPRAYF MSDTREEKRF LGEGHHRVQE NQMDKARRHP QGAWKELDRN YLNYGEEGAP GKWQQQGDLQ DTKENREEAR FQDKQYSSHH TAEKRKRLGE LFNPYYDPLQ WKSSHFERRD NMNDNFLEGE EENELTLNEK NFFPEYNYDW WEKKPFSEDV NWGYEKRNLA RVPKLDLKRQ YDRVAQLDQL LHYRKKSAEF PDFYDSEEPV STHQEAENEK DRADQTVLTE DEKKELENLA AMDLELQKIA EKFSQRG.

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

Description:

Myeloid Cell Leukemia Sequence 1 Human Recombinant

Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.

Product # :

PRO-1202

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

MCL1 Human Recombinant produced in E. coli is a single polypeptide chain containing 347 amino acids (1-327) and having a molecular mass of 37.2 kDa.MCL1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The MCL1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

More Info

Introduction
MCL1 is a member of the Bcl-2 family. MCL1 takes part in the control of apoptosis against cell existence, and in the preservation of viability but not of proliferation. Alternative splicing happens at this locus and two transcript variants encoding different isoforms are known. Isoform 1 is the longer gene product and it increases cell existence by inhibiting apoptosis. Isoform 2 is a shorter gene product which indorses apoptosis and is death-inducing.
Synonyms
Myeloid cell leukemia sequence 1 (BCL2-related), induced myeloid leukemia cell differentiation protein Mcl-1, myeloid cell leukemia ES, Bcl-2-related protein EAT/mcl1, Bcl-2-like protein 3, MCL1-ES, MCL1S, mcl1/EAT, BCL2L3, MCL1L.
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 MFGLKRNAVI GLNLYCGGAG LGAGSGGATR PGGRLLATEK EASARREIGG GEAGAVIGGS AGASPPSTLT PDSRRVARPP PIGAEVPDVT ATPARLLFFA PTRRAAPLEE MEAPAADAIM SPEEELDGYE PEPLGKRPAV LPLLELVGES GNNTSTDGSL PSTPPPAEEE EDELYRQSLE IISRYLREQA TGAKDTKPMG RSGATSRKAL ETLRRVGDGV QRNHETAFQG MLRKLDIKNE DDVKSLSRVM IHVFSDGVTN WGRIVTLISF GAFVAKHLKT INQESCIEPL AESITDVLVR TKRDWLVKQR GWDGFVEFFH VEDLEGG.

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

Description:

Vaccinia Related Kinase 3 Human Recombinant

Serine/threonine-protein pseudokinase VRK3, vaccinia related kinase 3, inactive serine/threonine-protein kinase VRK3.

Product # :

PRO-1130

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

VRK3 Human Recombinant produced in E. coli is a single polypeptide chain containing 497 amino acids (1-474) and having a molecular mass of 55.3 kDa.VRK3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The VRK3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 40% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
VRK3 is a member of the protein kinase superfamily. The VRK3 gene has replacements at a number of residues within the ATP binding motifs which in other kinases were proved to be required for catalysis in both human and mouse. In vitro assays show that VRK3 has no phosphorylation activity but probably holds its substrate binding capability. VRK3 is universally expressed in human tissues and its protein is restricts to the nucleus.
Synonyms
Serine/threonine-protein pseudokinase VRK3, vaccinia related kinase 3, inactive serine/threonine-protein kinase VRK3.
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 MGSMISFCPD CGKSIQAAFK FCPYCGNSLP VEEHVGSQTF VNPHVSSFQG SKRGLNSSFE TSPKKVKWSS TVTSPRLSLF SDGDSSESED TLSSSERSKG SGSRPPTPKS SPQKTRKSPQ VTRGSPQKTS CSPQKTRQSP QTLKRSRVTT SLEALPTGTV LTDKSGRQWK LKSFQTRDNQ GILYEAAPTS TLTCDSGPQK QKFSLKLDAK DGRLFNEQNF FQRAAKPLQV NKWKKLYSTP LLAIPTCMGF GVHQDKYRFL VLPSLGRSLQ SALDVSPKHV LSERSVLQVA CRLLDALEFL HENEYVHGNV TAENIFVDPE DQSQVTLAGY GFAFRYCPSG KHVAYVEGSR SPHEGDLEFI SMDLHKGCGP SRRSDLQSLG YCMLKWLYGF LPWTNCLPNT EDIMKQKQKF VDKPGPFVGP CGHWIRPSET LQKYLKVVMA LTYEEKPPYA MLRNNLEALL QDLRVSPYDP IGLPMVP

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

Description:

B-Cell Leukemia/Lymphoma 2 Human Recombinant (–BH2)

Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

Product # :

PRO-632

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
More Info

Description

Bcl-2 Des BH2 domain (187-202 residues) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 202 amino acids 1-186 and 203-218.The Bcl-2 is expressed as His-Tag fusion protein and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein contains 10mM Tris-HCL pH-8, 1mM EDTA and 250mM NaCl.

Purity

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

More Info

Introduction
BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.
Synonyms
Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Bcl-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Bcl-2 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
Suspend Bcl-2 in 100?l of 0.5M Acetic acid, over night at 4°C.
Dilute 10 fold into selected buffer system.
BCL-2 has tendency to form intramolecular disulfide bond, 5mM DTT is recommended in assay buffer. When running SDS-PAGE gel, 10mM DTT is recommended.
Applications
Input marker or positive control (Western Blotting).
Function study.

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

Description:

Crystallin, Mu Human Recombinant

Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

Product # :

PRO-2291

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

CRYM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 334 amino acids (1-314) and having a molecular mass of 35.9kDa. CRYM is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Crystallin, Mu (CRYM) is a taxon-specific crystallin protein which binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. CRYM doesn’t perform a structural role in lens tissue; instead CRYM binds thyroid hormone for possible regulatory or developmental roles. CRYM gene mutations are linked with autosomal dominant non-syndromic deafness. CRYM specifically catalyzes the reduction of imine bonds in brain substrates which may include cystathionine ketamine and lanthionine ketamine.
Synonyms
Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.
Physical Appearance
Sterile filtered colorless solution.
Stability
CRYM although stable at 4°C for 1 week, should be stored below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT VAAKLIYDSW SSGK

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

Description:

VEGF Co-regulated Chemokine 1 Rat Recombinant

Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.

Product # :

CHM-281

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

CXCL17 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, 300mM NaCl, pH 7.4.

Purity

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

Biological Activity

Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED₅₀ for this effect is typically 1-5 µg/ml.

More Info

Introduction
Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.
Synonyms
Protein Cxcl17, Cxcl17, RGD1304717, C-X-C motif chemokine 17, VEGF co-regulated chemokine 1, Vcc1, VCC-1.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.
Background
What is the molecular weight/Mw of CXCL17 RAT Protein?
CXCL17 RAT Protein has a total Mw of 11.5kDa.

What is the source or expression system of CXCL17 RAT Protein?
Escherichia Coli.

What is the Purity of CXCL17 RAT Protein?
CXCL17 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL17 RAT Protein?
Measured by its ability to induce VEGF expression in mouse endothelial cells. The ED50 for this effect is typically 1-5 µg/ml.

What is the amino acid sequence of CXCL17 RAT Protein?
SPNQEVARHH GDQHQAPRRW LWEGGQECDC KDWSLRVSKR KTTAVLEPPR KQCPCDHVKG SEKKNRRQKH HRKSQRPSRT CQQFLKRCQL ASFTLPL.

What applications can CXCL17 RAT Protein be used in?
CXCL17 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL17 RAT Protein?
The endotoxin level is minimal, CXCL17 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.

Description:

Mitochondrial Ribosomal Protein S23 Human Recombinant

Mitochondrial Ribosomal Protein S23, MRP-S23, S23mt, 28S Ribosomal Protein S23, Mitochondrial, CGI-138, HSPC329, MRPS23.

Product # :

PRO-2113

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

MRPS23 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a) and having a molecular mass of 24.2kDa.MRPS23 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MRPS23 protein solution (1mg/ml) containing Phosphate buffer saline (pH 7.4) and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
Mitochondrial Ribosomal Protein S23, also known as MRPS23 belongs to the mammalian mitochondrial ribosomal proteins which are encoded by nuclear genes and assist in proteinsynthesis inside the mitochondrion. Mitochondrial ribosomes consist of a small 28S subunit and a large 39S subunit. In addition, they have an estimated 75% protein to rRNA composition compared to prokaryotic ribosomes, where this ratio isreversed. An additional difference between mammalian mitoribosomes and prokaryotic ribosomes is that the lattercontain a 5S rRNA. Between different species, the proteins containing the mitoribosome differ very much in sequence, and occasionally in biochemical properties, which prevents easy recognition by sequence homology.
Synonyms
Mitochondrial Ribosomal Protein S23, MRP-S23, S23mt, 28S Ribosomal Protein S23, Mitochondrial, CGI-138, HSPC329, MRPS23.
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 MGSMAGSRLE TVGSIFSRTR DLVRAGVLKE KPLWFDVYDA FPPLREPVFQ RPRVRYGKAK APIQDIWYHE DRIRAKFYSV YGSGQRAFDL FNPNFKSTCQ RFVEKYTELQ KLGETDEEKL FVETGKALLA EGVILRRVGE ARTQHGGSHV SRKSEHLSVR PQTALEENET QKEVPQDQHL EAPADQSKGL LPP.

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

Description:

Bridging Integrator 1 Human Recombinant

AMPH2, AMPHL, MGC10367, SH3P9, Amphiphysin II.

Product # :

PRO-546

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

BIN1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 459 amino acids (1-439 a.a) and having a molecular mass of 50.4 kDa. The BIN1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BIN1 protein solution (1mg/ml) containing 20mM Tris buffer pH-8, 1mM DTT & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
BIN1 is a nucleocytoplasmic adaptor protein, one of which was primarily identified as MYC-interacting protein having the characteristics of a tumor suppressor. BIN1 protein interacts with and inhibits the oncogenic activity of the myc oncoprotein that is a key player in many human cancers. The absence of Bin1 contributes to growth deregulation in cancer cells in carcinoma of the breast, colon, lung, cervix, prostate and liver.
Synonyms
AMPH2, AMPHL, MGC10367, SH3P9, Amphiphysin II.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKAEEELIK AQKVFEEMNV DLQEELPSLW NSRVGFYVNT FQSIAGLEEN FHKEMSKLNQ NLNDVLVGLE KQHGSNTFTV KAQPSDNAPA KGNKSPSPPD GSPAATPEIR VNHEPEPAGG ATPGATLPKS PSQPAEASEV AGGTQPAAGA QEPGETAASE AASSSLPAVV VETFPATVNG TVEGGSGAGR LDLPPGFMFK VQAQHDYTAT DTDELQLRAG DVVLVIPFQN PEEQDEGWLM GVKESDWNQH KELEKCRGVF PENFTERVP.

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

Description:

Biogenesis of Lysosomal Organelles Complex-1, Subunit 2 Human Recombinant

Biogenesis of lysosomal organelles complex-1 subunit 2, BLOS2, BLOC-1 subunit 2, Centrosome-associated protein, centrosome protein oncogene, centrosomal 10 kDa protein, RP11-316M21.4, CEAP, FLJ30135, MGC10120.

Product # :

PRO-1094

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

BLOC1S2 Human Recombinant produced in E. coli is a single polypeptide chain containing 166 amino acids (1-142) and having a molecular mass of 18.5kDa.BLOC1S2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The BLOC1S2 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 50mM NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
BLOC1S2 is a member of the BLOC1S2 family. Biogenesis of lysosome-related organelles complex 1 or BLOC-1 is a universally expressed multisubunit protein complex which is essential for regular biogenesis of specialized organelles of the endosomal-lysosomal system, like melanosomes and platelet dense granules. BLOC1S2 takes part in cell proliferation.
Synonyms
Biogenesis of lysosomal organelles complex-1 subunit 2, BLOS2, BLOC-1 subunit 2, Centrosome-associated protein, centrosome protein oncogene, centrosomal 10 kDa protein, RP11-316M21.4, CEAP, FLJ30135, MGC10120.
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 MGSHMAAAAE GVLATRSDEP ARDDAAVETA EEAKEPAEAD ITELCRDMFS KMATYLTGEL TATSEDYKLL ENMNKLTSLK YLEMKDIAIN ISRNLKDLNQ KYAGLQPYLD QINVIEEQVA ALEQAAYKLD AYSKKLEAKY KKLEKR

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

Description:

Biliverdin Reductase B Human Recombinant

FLR, BVRB, SDR43U1, MGC117413, BLVRB, Flavin reductase, FR, NADPH-dependent diaphorase, NADPH-flavin reductase, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, Green heme-binding protein, GHBP.

Product # :

ENZ-387

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

BLVRB Human Recombinant amino produced in E.Coli is a single, non-glycosylated polypeptide chain containing 206 amino acids having a molecular mass of 22.1 kDa.The BLVRB is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein contains 20mM Tris-HCl buffer pH 8.5, 10% glycerol, and 1mM DTT.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
BLVRB (EC 1.3.1.24) catalyzes electron transfer from reduced pyridine nucleotides to flavins as well as methylene blue, pyrroloquinoline quinone, riboflavin, or methemoglobin. BLVRB is involved in protecting cells from oxidative damage or in regulating iron metabolism. BLVRB converts biliverdin to bilirubin in the liver, converting a double-bond between the second and third pyrrole ring into a single-bond. BLVRB plays a role as in human erythrocytic heme catabolic pathway and most mammalian species. Biliverdin reductase is abundantly expressed in kidney, spleen, liver and brain as well as at lower levels in the thymus and minimal levels being detected in testis.
Synonyms
FLR, BVRB, SDR43U1, MGC117413, BLVRB, Flavin reductase, FR, NADPH-dependent diaphorase, NADPH-flavin reductase, Biliverdin reductase B, BVR-B, Biliverdin-IX beta-reductase, Green heme-binding protein, GHBP.
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
MAVKKIAIFG ATGQTGLTTL AQAVQAGYEV TVLVRDSSRL PSEGPRPAHV VVGDVLQAAD VDKTVAGQDA VIVLLGTRND LSPTTVMSEG ARNIVAAMKA HGVDKVVACT SAFLLWDPTK VPPRLQAVTD DHIRMHKVLR ESGLKYVAVM PPHIGDQPLT GAYTVTLDGR GPSRVISKHD LGHFMLRCLT TDEYDGHSTY PSHQYQ.

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

Description:

BRAK (CXCL14) Rat Recombinant

C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.

Product # :

CHM-021

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

CXCL14 Rat Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CXCL14 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 RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

More Info

Introduction
CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.
Synonyms
C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
Background
What is the molecular weight/Mw of CXCL14 RAT Protein?
CXCL14 RAT Protein has a total Mw of 9.4kDa.

What is the source or expression system of CXCL14 RAT Protein?
Escherichia Coli.

What is the Purity of CXCL14 RAT Protein?
CXCL14 RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL14 RAT Protein?
Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

What is the amino acid sequence of CXCL14 RAT Protein?
SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.

What applications can CXCL14 RAT Protein be used in?
CXCL14 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL14 RAT Protein?
The endotoxin level is minimal, CXCL14 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.

Description:

Fibroblast Growth Factor-18 Rat Recombinant

Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.

Product # :

CYT-176

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info
sds-page

Description

FGF18 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 21.0kDa.The FGF 18 Rat is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2um filtered concentrated solution in PBS and 0.5M NaCl, pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

Biological Activity

The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×1,000,000 units/mg.

sds-page

More Info

Introduction
Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.
Synonyms
Fibroblast growth factor 18, FGF-18, zFGF5, Fgf18, D130055P09Rik.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FGF 18 Rat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF 18 Rat 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 FGF 18 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQTELQK PFKYTTVTKR SRRIRPTHPG
Background
What is the molecular weight/Mw of FGF18-RAT Protein?
FGF18-RAT Protein has a total Mw of 21kDa.

What is the source or expression system of FGF18-RAT Protein?
Escherichia Coli.

What is the Purity of FGF18-RAT Protein?
FGF18-RAT Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of FGF18-RAT Protein?
The ED50 as determined by the dose-dependent stimulation of thymidine uptake by BaF3 cells expressing FGF-receptors is < 0.5ng/ml, corresponding to a specific activity of > 2.0×1,000,000 units/mg.

What is the amino acid sequence of FGF18-RAT Protein?
EENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQTELQK PFKYTTVTKR SRRIRPTHPG

What applications can FGF18-RAT Protein be used in?
FGF18-RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for FGF18-RAT Protein?
The endotoxin level is minimal, FGF18-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.

Description:

Fractalkine Rat Recombinant (CX3CL1)

Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

Product # :

CHM-005

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Fractalkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa.The Fractalkine 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 97.0% as determined by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

More Info

Introduction
Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.
Synonyms
Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized FractalkineRat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fractalkine 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 Fractalkine in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG
Background
What is the molecular weight/Mw of CX3CL1 RAT Protein?
CX3CL1 RAT Protein has a total Mw of 8.7kDa.

What is the source or expression system of CX3CL1 RAT Protein?
Escherichia Coli.

What is the Purity of CX3CL1 RAT Protein?
CX3CL1 RAT Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CX3CL1 RAT Protein?
Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

What is the amino acid sequence of CX3CL1 RAT Protein?
QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG

What applications can CX3CL1 RAT Protein be used in?
CX3CL1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CX3CL1 RAT Protein?
The endotoxin level is minimal, CX3CL1 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.

Description:

B-cell CLL/lymphoma 7A Human Recombinant

B-cell CLL/lymphoma 7 protein family member A, BCL7A, BCL7.

Product # :

PRO-1318

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

BCL7A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 233 amino acids (1-210 a.a.) and having a molecular mass of 25.2kDa (Molecular size on SDS-PAGE will appear higher).BCL7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BCL7A protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol, 1mM DTT and 2mM EDTA.

Purity

Greater than 85% as determined by SDS-PAGE.

More Info

Introduction
B-cell CLL/lymphoma 7A (BCL7A) is a member of the BCL7 family. BCL7A is directly involved, with Myc and IgH, in a three-way gene translocation in a Burkitt lymphoma cell line. Thru gene translocation, the N-terminal region of the BCL7A gene is disrupted, which is assumed to be connected to the pathogenesis of a subset of high-grade B cell non-Hodgkin lymphoma. The N-terminal portion involved in the translocation includes the region which shares a compelling sequence similarity with those of BCL7B and BCL7C. Chromosomal anomalies involving BCL7A may be a cause of B-cell non-Hodgkin lymphoma.
Synonyms
B-cell CLL/lymphoma 7 protein family member A, BCL7A, BCL7.
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 MGSMSGRSVR AETRSRAKDD IKRVMAAIEK VRKWEKKWVT VGDTSLRIYK WVPVTEPKVD DKNKNKKKGK DEKCGSEVTT PENSSSPGMM DMHDDNSNQS SIADASPIKQ ENSSNSSPAP EPNSAVPSDG TEAKVDEAQA DGKEHPGAED ASDEQNSQSS MEHSMNSSEK VDRQPSGDSG LAAETSAISQ DLEGVPPSKK MKLEASQQNS EEM.

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

Description:

Transforming Growth Factor-Beta 2 Rat Recombinant

Transforming growth factor beta-2, TGF-beta-2, G-TSF, Tgfb-2, TGFbeta2.

Product # :

CYT-1267

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Transforming Growth Factor-Beta 2 Rat Recombinant produced in CHO is a homodimer, polypeptide chain containing 2 x 112 amino acids and having a total molecular mass of 25.4kDa.
TGFB2 Rat Recombinant is purified by proprietary chromatographic techniques.

Source

CHO Cells.

Formulation

The protein was lyophilized with 0.1% (v/v) TFA and 35% (v/v) Acetonitrile.

Purity

Greater than 97.0% as determined by SDS-PAGE and SEC-HPLC analyses.

Biological Activity

The biological activity was determined by TGFB2 ability to inhibit the mouse IL-4-dependent proliferation of mouse HT-2 cells. The expected ED50 for this effect is <0.05ng/ml, corresponding to a specific activity of ≥ 2.0 × 107 units/mg.

More Info

Synonyms
Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Transforming Growth Factor-Beta 2 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 Transforming Growth Factor-Beta 2 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
ALDAAYCFRN VQDNCCLRPL YIDFKRDLGW KWIHEPKGYN ANFCAGACPY LWSSDTQHTK VLSLYNTINP EASASPCCVS QDLEPLTILY YIGNTPKIEQ LSNMIVKSCK CS.
Background
Rat TGFB22 signals through TGFBR2, TGFBR1 using an accessory co-receptor TGFBR3 (betaglycan) that enhances presentation of TGFβ2
Rat TGFB2 is a potent inducer of epithelial–mesenchymal transition (EMT) therefore is used in Cancer metastasis, Fibrosis, Retinal disorders, Developmental biology and Wound healing

What is the source or expression system of Rat TGFB2 Protein?
CHO Cells

What is the Purity of Rat TGFB2 Protein?
Rat TGFB2 Protein is >97% pure as determined by SDS-PAGE.

What is the molecular weight / Mw of Rat TGFB2 Protein?
Rat TGFB2 Protein having a total Mw of 25.6kDa.

What is the Biological Activity of Rat TGFB2 Protein?
The biological functionality of Rat TGFB2 Protein is determined by mouse HT-2 cells.

What is the endotoxin level for Rat TGFB2 Protein?
The endotoxin level is minimal, Rat TGFB2 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of Rat TGF beta 2 Protein?
If there is sequence put it instead of the sentence

Is TGFB2 a homodimer / homodimeric protein?
Yes, TGFB1 is homo dimer consisting of 2 identical chains.

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

Description:

Biogenesis of Lysosomal Organelles Complex-1, Subunit 5 Human Recombinant

Biogenesis of lysosome-related organelles complex 1 subunit 5, BLOC-1 subunit 5, Protein Muted homolog, BLOC1S5, MUTED.

Product # :

PRO-1155

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

BLOC1S5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-187 a.a) and having a molecular mass of 24kDa.BLOC1S5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BLOC1S5 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 40% glycerol, 2mM DTT, 0.1mM PMSF and 1mM EDTA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

More Info

Introduction
Muted homolog (MUTED) is a component of the BLOC-1 complex, a complex which is necessary for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. The BLOC-1 complex is needed to steer membrane protein cargos into vesicles assembled at cell bodies for release into neurites and nerve terminals. In addition, this complex, along with SNARE proteins, is suggested to be involved in neurite extension. MUTED also interacts with pallidin, dystrobrevin binding protein 1 and CNO/cappuccino. MUTED is ubiquitously expressed with higher levels in the brain, bone marrow, kidney, and liver and lower levels in the skeletal muscle.
Synonyms
Biogenesis of lysosome-related organelles complex 1 subunit 5, BLOC-1 subunit 5, Protein Muted homolog, BLOC1S5, MUTED.
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 MGSMSGGGTE TPVGCEAAPG GGSKKRDSLG TAGSAHLIIK DLGEIHSRLL DHRPVIQGET RYFVKEFEEK RGLREMRVLE NLKNMIHETN EHTLPKCRDT MRDSLSQVLQ RLQAANDSVC RLQQREQERK KIHSDHLVAS EKQHMLQWDN FMKEQPNKRA EVDEEHRKAM ERLKEQYAEM EKDLAKFSTF.

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

Description:

Activin A Receptor Type 1 Human Recombinant

ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.

Product # :

CYT-1140

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info
sds-page

Description

ACVR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (21-123a.a.) and having a molecular mass of 38.4kDa. ACVR1 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

ACVR1 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.

sds-page

More Info

Introduction
Activin A Receptor Type 1 (ACVR1) is a member of TGF-beta serine/threonine kinase receptor family. ACVR1 forms a receptor complex contains2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate,bind and activate SMAD transcriptional regulators. ACVR1 takes part in left-right pattern formation during embryogenesis and is also essential in the BMP pathway which is responsible for the development and repair of the skeletal system.ACVR1 is linked to Fibrodysplasia Ossificans Progressiva which isknown for the formation of heterotopic bone throughout the body.
Synonyms
ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
Background
Functional Implications and Therapeutic Prospects of Activin A Receptor Type 1 Human Recombinant
1. Abstract
This study illuminates the functional roles and potential therapeutic applications of Activin A Receptor Type 1 Human Recombinant (ACVR1), a crucial protein in the TGF-beta superfamily signaling pathway. Through a comprehensive review of its structure, signaling mechanism, biological functions, and disease associations, this paper aims to elucidate the current understanding of ACVR1 and its potential therapeutic implications in various disease states.
2. Introduction
The Activin A Receptor Type 1 Human Recombinant, abbreviated as ACVR1, is a receptor protein vital for transmitting cellular signals in the Transforming Growth Factor-beta (TGF-beta) superfamily pathway. Known to play pivotal roles in organogenesis, bone growth, and cell differentiation, the ACVR1 and its functions present vast therapeutic potential.
3. Structure and Signaling of ACVR1
ACVR1 is a transmembrane serine/threonine kinase receptor, characterized by an extracellular ligand-binding domain and an intracellular kinase domain for signal transduction. Binding of ligands such as Activin A leads to the formation of heteromeric complexes with type II receptors, triggering phosphorylation events that activate downstream signaling pathways.
4. Biological Functions of ACVR1
Being a part of the TGF-beta superfamily signaling pathway, ACVR1 is implicated in a broad spectrum of biological processes. It is crucial for embryonic development, cellular proliferation, differentiation, apoptosis, and homeostasis. It also plays a significant role in bone morphogenesis, contributing to skeletal patterning and growth.
5. ACVR1 in Disease Pathology
The dysregulation of ACVR1 has been associated with various pathological conditions, including Fibrodysplasia Ossificans Progressiva (FOP), a rare genetic disorder characterized by progressive ossification of soft tissues. Mutations in ACVR1 lead to enhanced BMP signaling, causing aberrant bone formation. This highlights the critical role of ACVR1 in skeletal homeostasis and disease.
6. Therapeutic Potential of ACVR1
Given the central role of ACVR1 in cellular signaling and its association with disease, it presents a promising target for therapeutic intervention. Strategies to modulate ACVR1 signaling could potentially ameliorate symptoms of diseases like FOP, offering promising avenues for novel therapeutic approaches.
7. Conclusion and Future Perspectives
While our understanding of ACVR1's functional roles has expanded significantly over the years, much remains to be elucidated. Further research into the precise molecular mechanisms of ACVR1 and its pathway will pave the way for therapeutic advances, enhancing our capability to combat various diseases.
What is the molecular weight / Mw of ACVR1 Protein?
ACVR1 Protein has a total Mw of 38.4kDa.

What is the source or expression system of ACVR1 Protein?
Sf9, Baculovirus cells.

What is the Purity of ACVR1 Protein?
ACVR1 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of ACVR1 Protein?
The biological functionality of ACVR1 Protein will be determined in the future.

What is the endotoxin level for ACVR1 Protein?
The endotoxin level is minimal, ACVR1 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of ACVR1 Protein?
MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

What applications can ACVR1 Protein be used in?
ACVR1 Protein can probably be used in western blot, ELISA and Lateral Flow

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

Description:

Leptin Antagonist Triple Mutant Human Recombinant

Product # :

CYT-352

Price :

Quantity :

Shipping Method :

Shipped at Room temp

More Info

description
source
formulation
purity
biological activity
More Info

Description

Leptin Antagonist Triple Mutant Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular weight of 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A. Leptin Antagonist Triple Mutant Human Recombinant was purified by proprietary chromatographic techniques.

Source

Escherichia coli.

Formulation

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

Purity

Greater than 98.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.

Biological Activity

ProSpec’s Leptin triple antagonist is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

More Info

Physical Appearance
White lyophilized (freeze-dried) powder.
Stability
Lyophilized Leptin Antagonist Triple Mutant Human Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2 mg/ml and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Leptin Antagonist Triple Mutant Human Recombinant in sterile 0.4% NaHCO3, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

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

Description:

Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant

Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.

Product # :

CYT-679

Price :

Quantity :

Shipping Method :

Shipped with Ice Packs

More Info

description
source
formulation
purity
More Info

Description

TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 113 amino acids (279-390 a.a.) and having a total molecular mass of 12.9 kDa. TGF-b 1 (113 a.a.) is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

More Info

Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 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
MALDTNYCFS STEKNCCVRQ LYIDFRKDLG WKWIHEPKGY HANFCLGPCP YIWSLDTQYS KVLALYNQHN PGASAAPCCV PQALEPLPIVYYVGRKPKVE QLSNMIVRSC KCS.
Background
Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential
Abstract:

Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance.
Introduction:

TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications.
Production Process and Characteristics:

TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses.
Therapeutic Applications:

TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion.
Advantages and Challenges:

The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability.
Conclusion:

TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

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.

Country/region

Search results

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source

Formulation

Purity

Biological Activity

More Info

More Info

Description

Source

Formulation

Purity

More Info

More Info

Description

Source