Search results
1000 results found for “LIN Protein”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
S100A6 MurineDescription:
S100 Calcium Binding Protein A6 Mouse
Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.
Product # :
PRO-409Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
- Citations
Description
S100A6 also called Calcyclin has been purified by HPLC (see Kuznicki et al. (1989) Biochem. J. 263: 951-956).
Formulation
The protein was lyophilized from a concentrated solution (1mg/ml) containing no additives.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21.
S100A6 may function in stimulation of Ca2+-dependent insulin release, stimulation of prolactin secretion, and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma. -
Synonyms
Protein S100-A6, S100 calcium-binding protein A6, Calcyclin, Prolactin receptor-associated protein, 5B10, S100a6, Cacy, 2A9, PRA.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Mouse S100A6 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse S100A6 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 Mouse S100A6 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 :
ADAM10 Human, Sf9Description:
A Disintegrin and Metalloproteinase Domain 10 Human Recombinant, Sf9
Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.
Product # :
PRO-2359Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
ADAM10 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 467 amino acids (214-672 aa) and having a molecular mass of 51.6kDa (Migrates at 50-70kDa on SDS-PAGE under reducing conditions).ADAM10 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ADAM10 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
ADAM10 is part of the ADAM family which are cell surface proteins with a distinctive structure possessing both potential adhesion and protease domains. ADAM10 cleaves many proteins including TNF-alpha and E-cadherin. ADAM10 cleaves the membrane-bound precursor of tnf-alpha at 76- ala-|-val-77 to its mature soluble form. ADAM10 is in charge for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-a2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein ADAM10 is involved in the normal cleavage of the cellular prion protein. ADAM10 is involved in the cleavage of the adhesion molecule l1 at the cell surface and in the release of membrane vesicles, suggesting a vesicle-based protease activity. ADAM10 controls the proteolytic processing of notch and mediates lateral inhibition during neurogenesis.
-
Synonyms
Kuz, AD10, MADM, CD156c, HsT18717, ADAM metallopeptidase domain 10, A disintegrin and metalloproteinase domain 10, Mammalian disintegrin-metalloprotease, Kuzbanian protein homolog, CDw156, ADAM 10, ADAM10.
-
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
TTSAEKNTCQ LYIQTDHLFF KYYGTREAVI AQISSHVKAI DTIYQTTDFS GIRNISFMVK RIRINTTADE KDPTNPFRFP NIGVEKFLEL NSEQNHDDYC LAYVFTDRDF DDGVLGLAWV GAPSGSSGGI CEKSKLYSDG KKKSLNTGII TVQNYGSHVP PKVSHITFAH EVGHNFGSPH DSGTECTPGE SKNLGQKENG NYIMYARATS GDKLNNNKFS LCSIRNISQV LEKKRNNCFV ESGQPICGNG MVEQGEECDC GYSDQCKDEC CFDANQPEGR KCKLKPGKQC SPSQGPCCTA QCAFKSKSEK CRDDSDCARE GICNGFTALC PASDPKPNFT DCNRHTQVCI NGQCAGSICE KYGLEECTCA SSDGKDDKEL CHVCCMKKMD PSTCASTGSV QWSRHFSGRT ITLQPGSPCN DFRGYCDVFM RCRLVDADGP LARLKKAIFS PELYENIAEL EHHHHHH
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 :
SPOCK3 MouseDescription:
Sparc/Osteonectin 3 Mouse Recombinant
Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.
Product # :
PRO-2328Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
SPOCK3 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 423 amino acids (22-436 a.a.) and having a molecular mass of 47.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).SPOCK3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SPOCK3 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Testican-3 (Spock3) is a nervous system-expressed heparan sulfate proteoglycan belonging to a subgroup of the BM-40/SPARC/osteonectin family, whose role of in brain development is unclear. Spock3 inhibits the processing of pro-matrix metalloproteinase 2(MMP-2) by MT1-MMP and MT3-MMP. Spock3 is mostly confined to the developmental stage of the brain.
-
Synonyms
Testican-3, SPARC/osteonectin, CWCV, Kazal-like domains proteoglycan 3, Spock3.
-
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
AAAAVAVAGG RSDGGNFLDE KQWLTTISQY DKEVGQWNKF RDEVEDDYFR TWNPGKPFDQ ALDPAKDPCL KTKCSRHKVC ITQDAQTALC ISHRRLTHSM KEVGGSHKQW RGLPSSTCKP CPIAYASPVC GSDGHSYSSQ CKLEYQACVL GKQISIKCEG RCPCPSDKSM NIGRNVKRAC
SDLEFREVAN RLRDWFKALH ESGSQNKKTK ALLRPERSRF DTSILPICKD SLGWMFNRLD TNYDLLLDQS ELGSIYLDKN EQCTKAFFNS CDTYKDSLIS NNEWCYCFQR QQDPPCHTEL SNIQKRQGIK KLLGQYIPLC DEDGYYKPTQ CHGSVGQCWC VDRYGNEVVG SRINGVADCA
IDFEISGDFA SGDFREWTDD EGEEDDIMND KDDIEDDDED EGDDDDDGDV HDGYILEHHH HHH
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 :
AKT3 HumanDescription:
AKT Serine/Threonine Kinase 3 Human Recombinant
RAC-gamma serine/threonine-protein kinase, Protein kinase Akt-3, Protein kinase B gamma, PKB gamma, RAC-PK-gamma, STK-2, AKT3, PKBG.
Product # :
PKA-130Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
AKT3 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 485 amino acids (1-479a.a) and having a molecular mass of 56.5kDa.AKT3 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The AKT3 solution (0.25mg/ml) contains PBS (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
AKT Serine/Threonine Kinase 3 (Akt3) is a member of the Akt subfamily of serine/threonine protein kinases. Akt3is 1/3 closely related serine/threonine-protein kinases (Akt1, Akt2 and Akt3) called the Akt kinase and which regulate various processes including proliferation, metabolism, cell survival, growth and angiogenesis. The mentioned above is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Akt3 takes part in brain development and is critical for the viability of malignant glioma cells.
-
Synonyms
RAC-gamma serine/threonine-protein kinase, Protein kinase Akt-3, Protein kinase B gamma, PKB gamma, RAC-PK-gamma, STK-2, AKT3, PKBG.
-
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
MSDVTIVKEG WVQKRGEYIK NWRPRYFLLK TDGSFIGYKE KPQDVDLPYP LNNFSVAKCQ LMKTERPKPN TFIIRCLQWT TVIERTFHVD TPEEREEWTE AIQAVADRLQ RQEEERMNCS PTSQIDNIGE EEMDASTTHH KRKTMNDFDY LKLLGKGTFG KVILVREKAS GKYYAMKILK KEVIIAKDEV AHTLTESRVL KNTRHPFLTS LKYSFQTKDR LCFVMEYVNG GELFFHLSRE RVFSEDRTRF YGAEIVSALD YLHSGKIVYR DLKLENLMLD KDGHIKITDF GLCKEGITDA ATMKTFCGTP EYLAPEVLED NDYGRAVDWW GLGVVMYEMM CGRLPFYNQD HEKLFELILM EDIKFPRTLS SDAKSLLSGL LIKDPNKRLG GGPDDAKEIM RHSFFSGVNW QDVYDKKLVP PFKPQVTSET DTRYFDEEFT AQTITITPPE KYDEDGMDCM DNERRPHFPQ FSYSASGREH HHHHH.
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 :
FIBP HumanDescription:
FGF-1 Intracellular-Binding Protein Human Recombinant
FGFIBP, FIBP-1, Acidic fibroblast growth factor intracellular-binding protein, aFGF intracellular-binding protein, FGF-1 intracellular-binding protein, FIBP.
Product # :
CYT-758Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
- Citations
Description
FIBP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 387amino acids (1-364) and having a molecular mass of 44.3kDa. The FIBP is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
FIBP protein (0.5mg/ml) is supplied in 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
sds-page
Citations
More Info
-
Introduction
FGF-1 Intracellular-Binding Protein (FIBP) which is a member of Fibroblast growth factors (FGFs) binds to internalized FGF-1 and is thought to be involved in mitogenic function of FGF-1. FGF activity effects development, adult tissue homeostasis, angiogenesis and cancer progression. FIBP localizes to the nucleus and is greatly expressed in heart, skeletal muscle and pancreas and at lower levels in brain, placenta, liver and kidney.
-
Synonyms
FGFIBP, FIBP-1, Acidic fibroblast growth factor intracellular-binding protein, aFGF intracellular-binding protein, FGF-1 intracellular-binding protein, FIBP.
-
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 MGSMTSELDI FVGNTTLIDE DVYRLWLDGY SVTDAVALRV RSGILEQTGA TAAVLQSDTM DHYRTFHMLE RLLHAPPKLL HQLIFQIPPS RQALLIERYY AFDEAFVREV LGKKLSKGTK KDLDDISTKT GITLKSCRRQ FDNFKRVFKV VEEMRGSLVD NIQQHFLLSD RLARDYAAIV FFANNRFETG KKKLQYLSFG DFAFCAELMI QNWTLGAVGE APTDPDSQMD DMDMDLDKEF LQDLKELKVL VADKDLLDLH KSLVCTALRG KLGVFSEMEA NFKNLSRGLV NVAAKLTHNK DVRDLFVDLV EKFVEPCRSD HWPLSDVRFF LNQYSASVHS LDGFRHQALW DRYMGTLRGC LLRLYHD.
-
Background
What is the molecular weight/Mw of FIBP Protein?
FIBP Protein has a total Mw of 44.3kkDa.
What is the source or expression system of FIBP Protein?
Escherichia Coli.
What is the Purity of FIBP Protein?
FIBP Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FIBP Protein?
The biological functionality of FIBP Protein will be determined in the future.
What is the amino acid sequence of FIBP Protein?
MGSSHHHHHH SSGLVPRGSH MGSMTSELDI FVGNTTLIDE DVYRLWLDGY SVTDAVALRV RSGILEQTGA TAAVLQSDTM DHYRTFHMLE RLLHAPPKLL HQLIFQIPPS RQALLIERYY AFDEAFVREV LGKKLSKGTK KDLDDISTKT GITLKSCRRQ FDNFKRVFKV VEEMRGSLVD NIQQHFLLSD RLARDYAAIV FFANNRFETG KKKLQYLSFG DFAFCAELMI QNWTLGAVGE APTDPDSQMD DMDMDLDKEF LQDLKELKVL VADKDLLDLH KSLVCTALRG KLGVFSEMEA NFKNLSRGLV NVAAKLTHNK DVRDLFVDLV EKFVEPCRSD HWPLSDVRFF LNQYSASVHS LDGFRHQALW DRYMGTLRGC LLRLYHD.
What applications can FIBP Protein be used in?
FIBP Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FIBP Protein?
The endotoxin level is minimal, FIBP 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 :
POP4 HumanDescription:
Processing Of Precursor 4 Human Recombinant
RPP29, Ribonuclease P protein subunit p29, hPOP4.
Product # :
PRO-1407Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
POP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a.) and having a molecular mass of 27.8kDa.POP4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
POP4 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Processing of Precursor 4 (POP4) is a member of the eukaryotic/archaeal RNase P protein component 1 family. POP4 is one of the protein subunits of the small nucleolar ribonucleoprotein complexes: the endoribonuclease for mitochondrial RNA processing complex and the ribonuclease P complex. POP4 is confined to the nucleus and associates promptly with the RNA component of this complexes.POP4 is participating in processing of precursor RNAs.
-
Synonyms
RPP29, Ribonuclease P protein subunit p29, hPOP4.
-
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 MGSMKSVIYH ALSQKEANDS DVQPSGAQRA EAFVRAFLKR STPRMSPQAR EDQLQRKAVV LEYFTRHKRK EKKKKAKGLS ARQRRELRLF DIKPEQQRYS LFLPLHELWK QYIRDLCSGL KPDTQPQMIQ AKLLKADLHG AIISVTKSKC PSYVGITGIL LQETKHIFKI ITKEDRLKVI PKLNCVFTVE TDGFISYIYG SKFQLRSSER SAKKFKAKGT IDL.
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 :
SPON1 HumanDescription:
Recombinant Human Spondin-1
F-Spondin, VSGP
Product # :
pro-2758Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
SPON1 Human Recombinant produced in HEK293 cells is a single, glycosylated, polypeptide chain (29-807 a.a) containing a total of 785 amino acids, having a molecular mass of 88.9 kDa. SPON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
POR protein solution (0.25mg/ml) contains Phosphate buffer saline (pH 7.4) and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
SPON1 is a cell adhesion protein which take part in the regulation of protein binding activity, regulation of protein processing and regulation of amyloid precursor protein catabolic mechanism. SPON1 is found in the extracellular space and it co-localizes with collagen-containing extracellular matrix. SPON1 stimulates the attachment of spinal cord and sensory neuron cells and the outgrowth of neurites in vitro.
-
Synonyms
F-Spondin, VSGP
-
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
FSDETLDKVP KSEGYCSRIL RAQGTRREGY TEFSLRVEGD PDFYKPGTSY RVTLSAAPPS YFRGFTLIAL RENREGDKEE DHAGTFQIID EEETQFMSNC PVAVTESTPR RRTRIQVFWI APPAGTGCVI LKASIVQKRI IYFQDEGSLT KKLCEQDSTF DGVTDKPILD CCACGTAKYR LTFYGNWSEK THPKDYPRRA NHWSAIIGGS HSKNYVLWEY GGYASEGVKQ VAELGSPVKM EEEIRQQSDE VLTVIKAKAQ WPAWQPLNVR AAPSAEFSVD RTRHLMSFLT MMGPSPDWNV GLSAEDLCTK ECGWVQKVVQ DLIPWDAGTD SGVTYESPNK PTIPQEKIRP LTSLDHPQSP FYDPEGGSIT QVARVVIERI ARKGEQCNIV PDNVDDIVAD LAPEEKDEDD TPETCIYSNW SPWSACSSST CDKGKRMRQR MLKAQLDLSV PCPDTQDFQP CMGPGCSDED GSTCTMSEWI TWSPCSISCG MGMRSRERYV KQFPEDGSVC TLPTEETEKC TVNEECSPSS CLMTEWGEWD ECSATCGMGM KKRHRMIKMN PADGSMCKAE TSQAEKCMMP ECHTIPCLLS PWSEWSDCSV TCGKGMRTRQ RMLKSLAELG DCNEDLEQVE KCMLPECPID CELTEWSQWS ECNKSCGKGH VIRTRMIQME PQFGGAPCPE TVQRKKCRIR KCLRNPSIQK LRWREARESR RSEQLKEESE GEQFPGCRMR PWTAWSECTK LCGGGIQERY MTVKKRFKSS QFTSCKDKKE IRACNVHPC-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 :
THRSP HumanDescription:
Thyroid Hormone Responsive Human Recombinant
Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 protein.
Product # :
PRO-1485Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
THRSP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146 a.a.) and having a molecular mass of 18.9kDa.THRSP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
THRSP protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.15M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Thyroid Hormone Responsive (THRSP) is a member of the SPOT14 family. THRSP is similar to the gene product of S14, a rat gene whose expression is limited to liver and adipose tissue and is controlled by nutritional and hormonal factors. THRSP is expressed in liver and adipocytes, specifically in lipomatous modules. In addition It is expressed in lipogenic breast cancers, which suggests a role in controlling tumor lipid metabolism.
-
Synonyms
Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 protein.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMQVLTKR YPKNCLLTVM DRYAAEVHNM EQVVMIPSLL RDVQLSGPGG QAQAEAPDLY TYFTMLKAIC VDVDHGLLPR EEWQAKVAGS EENGTAETEE VEDESASGEL DLEAQFHLHF SSLHHILMHL TEKAQEVTRK YQEMTGQVW.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SIRT1 HumanDescription:
Sirtuin-1 Human Recombinant
Sirtuin 1, SIRT1, SIR2L1, Regulatory Protein SIR2 Homolog 1, hSIR2, hSIRT1, SIR2-Like Protein 1, SIR2alpha, NAD-Dependent Deacetylase Sirtuin-1, NAD-Dependent Protein Deacetylase Sirtuin-1, Sir2-Like 1, Sirtuin Type 1, EC 3.5.1.-.
Product # :
PRO-1909Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
SIRT1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 280 amino acids (254-495) and having a molecular mass of 31.6 kDa.SIRT1 is fused to a 38 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The SIRT1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Sirtuin-1 (SIRT1) belongs to the sirtuin family of proteins, homologs to the yeast Sir2 protein. Sirtuin family members are characterized by a sirtuin core domain and grouped into 4 classes. The functions of human sirtuins have not yet been established; though, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. It has been proposed that the human sirtuins may serve as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity.
-
Synonyms
Sirtuin 1, SIRT1, SIR2L1, Regulatory Protein SIR2 Homolog 1, hSIR2, hSIRT1, SIR2-Like Protein 1, SIR2alpha, NAD-Dependent Deacetylase Sirtuin-1, NAD-Dependent Protein Deacetylase Sirtuin-1, Sir2-Like 1, Sirtuin Type 1, EC 3.5.1.-.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMKK IIVLTGAGVS VSCGIPDFRS RDGIYARLAV DFPDLPDPQA MFDIEYFRKD PRPFFKFAKE IYPGQFQPSL CHKFIALSDK EGKLLRNYTQ NIDTLEQVAG IQRIIQCHGS FATASCLICK YKVDCEAVRG DIFNQVVPRC PRCPADEPLA IMKPEIVFFG ENLPEQFHRA MKYDKDEVDL LIVIGSSLKV RPVALIPSSI PHEVPQILIN REPLPHLHFD VELLGDCDVI INELCHRLGG.
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 :
HAND1 HumanDescription:
Heart and Neural Crest Derivatives Expressed 1 Human Recombinant
Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.
Product # :
PRO-1231Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
HAND1 Human Recombinant produced in E. coli is a single polypeptide chain containing 238 amino acids (1-215) and having a molecular mass of 26.0 kDa.HAND1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The HAND1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
HAND1 is a member of the basic helix-loop-helix family of transcription factors. HAND1 is one of two HAND proteins, two closely related family members that are irregularly expressed in the emerging ventricular chambers and have a key part in cardiac morphogenesis. Operating in a complementary manner, they work in the development of the right ventricle and aortic arch arteries, implicating them as mediators of congenital heart disease. Furthermore, HAND1 is obligatory for early trophoblast differentiation.
-
Synonyms
Heart- And Neural Crest Derivatives-Expressed Protein 1, Extraembryonic Tissues Heart Autonomic Nervous System And Neural Crest Derivatives-Expressed Protein 1, Class A Basic Helix-Loop-Helix Protein 27, BHLHa27, EHAND, Thing1, Hxt.
-
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 MGSMNLVGSY AHHHHHHHPH PAHPMLHEPF LFGPASRCHQ ERPYFQSWLL SPADAAPDFP AGGPPPAAAA AATAYGPDAR PGQSPGRLEA LGGRLGRRKG SGPKKERRRT ESINSAFAEL RECIPNVPAD TKLSKIKTLR LATSYIAYLM DVLAKDAQSG DPEAFKAELK KADGGRESKR KRELQQHEGF PPALGPVEKR IKGRTGWPQQ VWALELNQ
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 :
FGF 9 RatDescription:
Fibroblast Growth Factor-9 Rat Recombinant
GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.
Product # :
CYT-558Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
Rat FGF9 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 207 amino acids and having a molecular mass of 23.3kDa.The FGF-9 Mouse Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FGF-9 was lyophilized from a concentrated (1mg/ml) sterile solution containing 10mM NaP, pH-7.5 &, 75mM Ammonium Sulfate.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.Citations
More Info
-
Introduction
Rat and mouse FGF-9 show a very high homology to human FGF-9. The transcripts for FGF-9 have been found in brain and in kidney tissue. Fibroblast Growth Factor-9 is a member of the fibroblast growth factor (FGF) family. FGF family members possess broad mitogenic and cell survival activities, and are involved in a variety of biological processes, including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF9 was isolated as a secreted factor that exhibits a growth-stimulating effect on cultured glial cells. In nervous system, this protein is produced mainly by neurons and may be important for glial cell development. Expression of the mouse homolog of this gene was found to be dependent on Sonic hedgehog (Shh) signaling. Mice lacking the homolog gene displayed a male-to-female sex reversal phenotype, which suggested a role in testicular embryogenesis Fibroblast Growth Factor 9 may have a role in glial cell growth and differentiation during development, gliosis during repair and regeneration of brain tissue after damage, differentiation and survival of neuronal cells, and growth stimulation of glial tumors.
-
Synonyms
GAF (Glia-activating factor), HBGF-9, MGC119914, MGC119915, FGF-9.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Rat Fibroblast Growth Factor-9 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF9 Rat Recombinant 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 Rat FGF-9 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MPLGEVGSYFG VQDAVPFGNV PVLPVDSPVL LNDHLGQSEA GGLPRGPAVT DLDHLKGILR RRQLYCRTGF HLEIFPNGTI QGTRKDHSRF GILEFISIAV GLVSIRGVDS GLYLGMNEKG ELYGSEKLTQ ECVFREQFEE NWYNTYSSNL YKHVDTGRRY YVALNKDGTP REGTRTKRHQ KFTHFLPRPV DPDKVPELYK DILSQS.
-
Background
What is the molecular weight/Mw of FGF9 Protein?
FGF9 Protein has a total Mw of 23.3kDa.
What is the source or expression system of FGF9 Protein?
Escherichia Coli.
What is the Purity of FGF9 Protein?
FGF9 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF9 Protein?
The ED50, calculated by the dose-dependant proliferation of BAF3 cells expressing FGF receptors (measured by 3H-thymidine uptake) is <0.5 ng/ml, corresponding to a specific activity of 2,000,000 Units/mg.
What is the amino acid sequence of FGF9 Protein?
MPLGEVGSYFG VQDAVPFGNV PVLPVDSPVL LNDHLGQSEA GGLPRGPAVT DLDHLKGILR RRQLYCRTGF HLEIFPNGTI QGTRKDHSRF GILEFISIAV GLVSIRGVDS GLYLGMNEKG ELYGSEKLTQ ECVFREQFEE NWYNTYSSNL YKHVDTGRRY YVALNKDGTP REGTRTKRHQ KFTHFLPRPV DPDKVPELYK DILSQS.
What applications can FGF9 Protein be used in?
FGF9 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF9 Protein?
The endotoxin level is minimal, FGF9 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 :
TNNI1 Human NativeDescription:
Troponin I Skeletal Muscle Human
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.
Product # :
PRO-2789Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
TNNI1 Native produced in Human skeletal is Immunological identity confirmed by reaction with monoclonal antibody that is specific for the Human Troponin I Skeletal Muscle. TNNI1 Native is purified by proprietary chromatographic technique.
Source
Human skeletal muscle.
Formulation
TNNI1 was lyophilized from 0.01M HCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Synonyms
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Troponin I Skeletal Muscle although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI1 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 TNNI1 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
Troponin I, specifically the skeletal muscle isoform encoded by the TNNI1 gene, is a crucial regulator of muscle contraction. It functions as part of the troponin complex, which controls the interaction between actin and myosin filaments during muscle contraction. While extensive research has been conducted on troponin I in the context of cardiac muscle and cardiac diseases, the study of native human skeletal muscle troponin I remains an important but relatively understudied area. This research aims to provide a comprehensive exploration of native human skeletal muscle troponin I (TNNI1), elucidating its functions, structural significance, and potential applications in musculoskeletal research and clinical medicine.
The primary objective of this research is to elucidate the physiological role of native human skeletal muscle TNNI1 in muscle contraction. Experiments involving human skeletal muscle tissue samples and isolated muscle fibers will be conducted to investigate how TNNI1 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of skeletal muscle physiology and its implications for musculoskeletal health.
The second objective is to assess the clinical relevance of native TNNI1 in muscle-related diseases. Clinical studies involving patients with various neuromuscular and muscle-wasting conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI1 as a biomarker. These investigations may provide valuable insights into the use of native TNNI1 in the early detection and management of muscle disorders.
The third objective is to explore the potential applications of native TNNI1 in musculoskeletal research and therapeutic development. Research will investigate the use of native TNNI1-expressing cells and tissues as models for studying muscle disorders and for developing novel therapeutic interventions targeting the troponin complex.
By delving into the functions and roles of native human skeletal muscle TNNI1, this research aims to expand our knowledge of skeletal muscle physiology, its implications for muscle-related diseases, and its potential applications in musculoskeletal research and clinical medicine.
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 :
TAX1BP3 HumanDescription:
Tax1 Binding Protein 3 Human Recombinant
Tax1 (human T-cell leukemia virus type I) binding protein 3, TIP-1, Glutaminase-interacting protein 3, Tax interaction protein 1.
Product # :
PRO-981Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
TAX1BP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 144 amino acids (1-124 a.a.) and having a molecular mass of 15.8kDa.TAX1BP3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
TAX1BP3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TAX1BP3 holds one PDZ domain, which uses for interactions with other proteins like the interaction with the C-terminus of Rhotekin that facilitates Rho-mediated activation of the FOS serum response element. In addition, PDZ domain interacts with beta-catenin to inhibit the transcriptional activity of beta-catenin. TAX1BP3 exists in several cell lines, such as HeLa, and is expressed in small quantities in peripheral blood leukocytes.
-
Synonyms
Tax1 (human T-cell leukemia virus type I) binding protein 3, TIP-1, Glutaminase-interacting protein 3, Tax interaction 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 MSYIPGQPVT AVVQRVEIHK LRQGENLILG FSIGGGIDQD PSQNPFSEDK TDKGIYVTRV SEGGPAEIAG LQIGDKIMQV NGWDMTMVTH DQARKRLTKR SEEVVRLLVT RQSLQKAVQQ SMLS.
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 :
RQCD1 HumanDescription:
RCD1 Required for Cell Differentiation1 Human Recombinant
Cell differentiation protein RCD1 homolog, Rcd-1, RQCD1, RCD1, CNOT9, CT129, RCD1+.
Product # :
PRO-008Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
RQCD1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 319 amino acids (1-299 a.a.) and having a molecular mass of 35.7kDa. The RQCD1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RQCD1 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
RQCD1 is a novel transcriptional cofactor which mediates retinoic acid-induced cell differentiation. RQCD1 down-regulates MYB- and JUN-dependent transcription and may have a role in cell differentiation. RQCD1 also has a role in retinoic acid-controlled lung development.
-
Synonyms
Cell differentiation protein RCD1 homolog, Rcd-1, RQCD1, RCD1, CNOT9, CT129, RCD1+.
-
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 MHSLATAAPV PTTLAQVDRE KIYQWINELS SPETRENALL ELSKKRESVP DLAPMLWHSF GTIAALLQEI VNIYPSINPP TLTAHQSNRV CNALALLQCV ASHPETRSAF LAAHIPLFLY PFLHTVSKTR PFEYLRLTSL GVIGALVKTD EQEVINFLLT TEIIPLCLRI MESGSELSKT VATFILQKIL LDDTGLAYIC QTYERFSHVA MILGKMVLQL SKEPSARLLK HVVRCYLRLS DNPRAREALR QCLPDQLKDT TFAQVLKDDT TTKRWLAQLV KNLQEGQVTD PRGIPLPPQ.
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 :
PELI2 HumanDescription:
Pellino E3 Ubiquitin Protein Ligase Family Member 2 Human Recombinant
Pellino E3 Ubiquitin Protein Ligase Family Member 2, Pellino-2, E3 Ubiquitin-Protein Ligase Pellino Homolog 2, Pellino (Drosophila) Homolog 2, Pellino Homolog 2 (Drosophila), Protein Pellino Homolog 2, Pellino Homolog 2, EC 6.3.2, PELI2.
Product # :
PRO-2066Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
PELI2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 443 amino acids (1-420 a.a) and having a molecular mass of 48.8kDa. PELI2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PELI2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Pellino E3 Ubiquitin Protein Ligase Family Member 2, also known as PELI2 is an E3 ubiquitin ligase which catalyzes the covalent attachment of ubiquitin moieties onto substrate proteins. PELI2 is implicated in the TLR and IL-1 signaling pathways through interaction with the complex which contain IRAK kinases and TRAF6. PELI2 also mediates IL1B-induced IRAK1 'Lys-63'-linked polyubiquitination and possibly 'Lys-48'-linked ubiquitination. PELI2 is significant for LPS- and IL1B-induced MAP3K7-dependent, however not for MAP3K3-dependent, NF-kappa-B activation. Moreover, PELI2 can activate the MAP (mitogen activated protein) kinase pathway directing to activation of ELK1.
-
Synonyms
Pellino E3 Ubiquitin Protein Ligase Family Member 2, Pellino-2, E3 Ubiquitin-Protein Ligase Pellino Homolog 2, Pellino (Drosophila) Homolog 2, Pellino Homolog 2 (Drosophila), Protein Pellino Homolog 2, Pellino Homolog 2, EC 6.3.2, PELI2.
-
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 MGSMFSPGQE EHCAPNKEPV KYGELVVLGY NGALPNGDRG RRKSRFALYK RPKANGVKPS TVHVISTPQA SKAISCKGQH SISYTLSRNQ TVVVEYTHDK DTDMFQVGRS TESPIDFVVT DTISGSQNTD EAQITQSTIS RFACRIVCDR NEPYTARIFA AGFDSSKNIF LGEKAAKWKN PDGHMDGLTT NGVLVMHPRG GFTEESQPGV WREISVCGDV YTLRETRSAQ QRGKLVESET NVLQDGSLID LCGATLLWRT ADGLFHTPTQ KHIEALRQEI NAARPQCPVG LNTLAFPSIN RKEVVEEKQP WAYLSCGHVH GYHNWGHRSD TEANERECPM CRTVGPYVPL WLGCEAGFYV DAGPPTHAFT PCGHVCSEKS AKYWSQIPLP HGTHAFHAAC PFCATQLVGE QNCIKLIFQG PID.
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 :
ProSpec 7-Band MarkerDescription:
ProSpec 8.5, 13.5, 18, 28, 40, 57 & 70 kDa Protein Marker
Protein Marker, Protein Ladder, Protein Standard, Mw Marker, Mw ladder, Mw Standard
Product # :
pro-2654Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- More Info
- Citations
Description
ProSpec 7-Protein marker containing 8.5, 13.5, 18, 28, 40, 57 & 70 kDa. The recombinant proteins are produced in E.Coli is and purified by proprietary chromatographic techniques.
Source
E.Coli
Formulation
ProSpec 7-protein marker solution (0.5ug/ul/protein) contains 12mM Tris-HCl pH-6.8, 5% glycerol, 0.4% SDS 2.88mM 2-mercaptoethanol & 0.02% bromophenol blue.
Citations
More Info
-
Synonyms
Protein Marker, Protein Ladder, Protein Standard, Mw Marker, Mw ladder, Mw Standard
-
Physical Appearance
Sterile Filtered blue 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. Avoid multiple freeze-thaw cycles.
-
Molecular Weight
Use 5ul per lane. There is no need to heat before use. Each Protein conc. is 0.5ug/ul.
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 :
REG1B HumanDescription:
Regenerating Islet-Derived 1 Beta Human Recombinant
Lithostathine-1-beta, Regenerating protein I beta, REG1B, REGL.
Product # :
PRO-391Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
The Recombinant Human REG 1 beta manufactured with N-terminal fusion of His Tag. The Human REG 1 beta His-Tagged Fusion Protein, produced in E. coli, is 17.8 kDa protein containing 144 amino acid residues of the Human REG 1 beta and 12 additional amino acid residues – His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 20mM Tris, pH 8.0.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Reg protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
Reg I was found to be expressed mainly in pancreatic beta and acinoductular cells as well as gastric fundic enterochromaffin-like (ECL) cells. Reg I production in ECL cells is stimulated by gastrin, as well as by the proinflammatory cytokine, cytokine-induced neutrophil chemoattractant (CINC)-2Beta. In patients with chronic hypergastrinemia, Reg production is stimulated, with the increased proliferation of gastric mucosal cells. Patients with Helicobacter pylori infection also showed increased Reg production in the gastric mucosa, partly via increased plasma gastrin concentration and partly via increased proinflammatory cytokine production. The serum concentration of the reg-protein was significantly higher in patients with various pancreatic diseases than in normal controls, and was also significantly higher in patients with acute pancreatitis or chronic relapsing pancreatitis than in patients with chronic pancreatitis. Furthermore, the serum PSP/reg-protein concentration was also significantly increased in liver cirrhosis, choledocholithiasis, and various cancers of the digestive system. -
Synonyms
Lithostathine-1-beta, Regenerating protein I beta, REG1B, REGL.
-
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 a working concentration approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHAS HMQESQTELP NPRISCPEGT NAYRSYCYYF NEDPETWVDA DLYCQNMNSG NLVSVLTQAE GAFVASLIKE SSTDDSNVWI GLHDPKKNRR WHWSSGSLVS YKSWDTGSPS SANAGYCASL TSCSGFKKWK DESCEKKFSF VCKFKN.
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 :
CXCL14 Human, HisDescription:
BRAK Human Recombinant (CXCL14), His-Tag
C-X-C motif chemokine 14, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
Product # :
CHM-239Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
CXCL14 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10.66 kDa. The Human BRAK contains a 10 a.a. fusion His tag at N-Terminus. The BRAK is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CXCL14 filtered (0.4µm) and lyophilized from a concentrated (0.5mg/ml) solution containing 20mM Tris buffer & 20mM NaCl pH-7.5.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Citations
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, Small-inducible cytokine B14, Chemokine BRAK, Bolekine, NJAC, KS1, Kec, BMAC, MIP-2g, SCYB14, CXCL14, BRAK, MGC10687.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BRAK although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BRAK 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 CXCL14 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHAS SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS VSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
-
Background
What is the molecular weight/Mw of CXCL14 HUMAN, HIS Protein?
CXCL14 HUMAN, HIS Protein has a total Mw of 10.66kDa.
What is the source or expression system of CXCL14 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of CXCL14 HUMAN, HIS Protein?
CXCL14 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of CXCL14 HUMAN, HIS Protein?
The biological functionality of CXCL14 HUMAN, HIS Protein will be determined in the future.
What is the amino acid sequence of CXCL14 HUMAN, HIS Protein?
MKHHHHHHAS SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS VSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.
What applications can CXCL14 HUMAN, HIS Protein be used in?
CXCL14 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CXCL14 HUMAN, HIS Protein?
The endotoxin level is minimal, CXCL14 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL14 HUMAN, HIS that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.
Where can I order bulk mg quantities of CXCL14 HUMAN, HIS?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BMP3 HumanDescription:
Bone Morphogenetic protein-3 Human Recombinant
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
Product # :
CYT-937Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Citations
Description
BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.
Purity
Greater than 95.0% as determined by: (a) Analysis by HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.Citations
More Info
-
Introduction
Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.
-
Synonyms
Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
-
Background
Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration
Abstract:
Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.
Introduction:
Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.
Characteristics and Signaling Pathways:
BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.
Production of BMP-3 Human Recombinant:
Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.
Potential Therapeutic Applications:
BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.
Conclusion:
BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.
What is the molecular weight/Mw of BMP3 Protein?
BMP3 Protein has a total Mw of 24.8kDa.
What is the source or expression system of BMP3 Protein?
Escherichia Coli.
What is the Purity of BMP3 Protein?
BMP3 Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of BMP3 Protein?
The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.
What is the amino acid sequence of BMP3 Protein?
QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.
What applications can BMP3 Protein be used in?
BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BMP3 Protein?
The endotoxin level is minimal, BMP3 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MAPT HumanDescription:
Microtubule-Associated Protein Tau Human Recombinant
TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.
Product # :
PRO-295Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
MAPT Recombinant Human (Isoform-4) produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (1-352 a.a.) and having a molecular mass of 38.9 kDa (Real molecular weight on SDS-PAGE will be shift up). The MAPT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
MAPT is a neuronal microtubule associated protein localized mostly on axons.
MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain. -
Synonyms
TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.
-
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 MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL.
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 :
TPPP3 HumanDescription:
Tubulin Polymerization-Promoting Protein Family Member 3 Human Recombinant
Tubulin Polymerization-Promoting Protein Family Member 3, Brain Specific Protein, p25gamma, TPPP/p20, p20.
Product # :
PRO-1615Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
TPPP3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-176) and having a molecular mass of 21.4kDa.TPPP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TPPP3 solution contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
TPPP3 is a member of the TPPP family and is found in the cytoplasm. TPPP3 binds tubulin, has microtubule bundling activity takes part in mitosis and cell proliferation.
-
Synonyms
Tubulin Polymerization-Promoting Protein Family Member 3, Brain Specific Protein, p25gamma, TPPP/p20, p20.
-
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 MGSMAASTDM AGLEESFRKF AIHGDPKASG QEMNGKNWAK LCKDCKVADG KSVTGTDVDI VFSKVKGKSA RVINYEEFKK ALEELATKRF KGKSKEEAFD AICQLVAGKE PANVGVTKAK TGGAVDRLTD TSRYTGSHKE RFDESGKGKG IAGRQDILDD SGYVSAYKNA GTYDAKVKK
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 :
ST13 HumanDescription:
HSP70 Interacting Protein Human Recombinant
AAG2, SNC6, HSPABP, FAM10A1, FAM10A4, HSPABP1, ST-13, Hsc70-interacting protein, Suppression of tumorigenicity protein 13, Putative tumor suppressor ST13, Protein FAM10A1, Progesterone receptor-associated p48 protein, Renal carcinoma antigen NY-REN-33, ST13, HIP, HOP, P48, PRO0786, FLJ27260, MGC129952.
Product # :
HSP-130Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
Recombinant Human ST13 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 369 amino acids (12-369 a.a.) and having a molecular mass of 41.3kDa.ST13 human recombinant is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The ST13 protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT, 0.1M NaCl & 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
ST13 is an adaptor protein (co-chaperone) that mediates the association of HSP70 & HSP90 and appears in early receptor complexes. ST13 plays a role in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. The expression of ST13 is downregulated in colorectal carcinoma tissue signifying that is candidate tumor suppressor gene. Through common binding to both Hsp70 and Hsp90, ST13 functions as an adaptor that can integrate Hsp70 and Hsp90 interactions. The expression of ST13 decreases in colorectal cancer tissue compared with that in adjacent normal tissue. ST13 is mostly expressed in colorectal epithelia and adenocarcinoma cells. ST13 functions to promote the efficiency of glucocorticoid receptor maturation in cells. The expression levels of the ST13 gene were significantly decreased in primary tumors compared with adjacent mucosa.
-
Synonyms
AAG2, SNC6, HSPABP, FAM10A1, FAM10A4, HSPABP1, ST-13, Hsc70-interacting protein, Suppression of tumorigenicity protein 13, Putative tumor suppressor ST13, Protein FAM10A1, Progesterone receptor-associated p48 protein, Renal carcinoma antigen NY-REN-33, ST13, HIP, HOP, P48, PRO0786, FLJ27260, MGC129952.
-
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
MDPRKVNELR AFVKMCKQDP SVLHTEEMRF LREWVESMGG KVPPATQKAK SEENTKEEKP DSKKVEEDLK ADEPSSEESD LEIDKEGVIEPDTDAPQEMG DENAEITEEM MDQANDKKVA AIEALNDGEL QKAIDLFTDA IKLNPRLAIL YAKRASVFVK LQKPNAAIRD CDRAIEINPD SAQPYKWRGK AHRLLGHWEE AAHDLALACK LDYDEDASAM LKEVQPRAQK IAEHRRKYER KREEREIKER IERVKKAREE HERAQREEEA
RRQSGAQYGS FPGGFPGGMP GNFPGGMPGM GGGMPGMAGM PGLNEILSDP EVLAAMQDPE VMVAFQDVAQ NPANMSKYQS NPKVMNLISK LSAKFGGQA.
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 :
RUNX3 HumanDescription:
Runt-Related Transcription Factor 3 Human Recombinant
AML2, CBFA3, PEBP2aC, PEBP2A3, FLJ34510, MGC16070, RUNX3, Oncogene AML-2, Runt-related transcription factor 3, Core-binding factor subunit alpha-3, Acute myeloid leukemia 2 protein, Polyomavirus enhancer-binding protein 2 alpha C subunit, SL3-3 enhancer factor 1 alpha C subunit, SL3/AKV core-binding factor alpha C subunit.
Product # :
PRO-836Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
RUNX3 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (53-186 a.a.) and having a molecular mass of 17.1 kDa. The RUNX3 is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
RUNX3 Human solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
RUNX3 is part of the RUNX family that mediates the expression of genes which participate in cellular differentiation and cell cycle progression. RUNX3 heterodimer and the beta subunit form a complex that binds to the core DNA sequence 5''-PYGPYGGT-3'' found in several enhancers and promoters, and can either activate or suppress transcription. RUNX3 interacts with additional transcription factors. RUNX3 is a good candidate for gastric cancer tumor suppressor diagnosis.
-
Synonyms
AML2, CBFA3, PEBP2aC, PEBP2A3, FLJ34510, MGC16070, RUNX3, Oncogene AML-2, Runt-related transcription factor 3, Core-binding factor subunit alpha-3, Acute myeloid leukemia 2 protein, Polyomavirus enhancer-binding protein 2 alpha C subunit, SL3-3 enhancer factor 1 alpha C subunit, SL3/AKV core-binding factor alpha C subunit.
-
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 MRSMVDVLAD HAGELVRTDS PNFLCSVLPS HWRCNKTLPV AFKVVALGDV PDGTVVTVMA GNDENYSAEL RNASAVMKNQ VARFNDLRFV GRSGRGKSFT LTITVFTNPT QVATYHRAIK VTVDGPREPR RHRQK.
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 :
MYL5 HumanDescription:
Myosin Light Chain 5 Human Recombinant
Myosin light chain 5, Myosin regulatory light chain 5, Superfast myosin regulatory light chain 2, MYLC2, MyLC-2, MYL5.
Product # :
PRO-916Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- Citations
Description
MYL5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-132 a.a.) and having a molecular mass of 17.4kDa.MYL5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYL5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) containing 1mM DTT, 30% glycerol and 0.1M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Citations
More Info
-
Introduction
Myosin regulatory light chain 5 (MYL5) is a hexameric ATPase cellular motor protein. Myosin is comprised of 2 heavy chains, 2 nonphosphorylatable alkali light chains, and 2 phosphorylatable regulatory light chains. MYL5 is a regulatory light chain and is expressed in the fetal muscle and in the adult retina, cerebellum, and basal ganglia. The reconstitution of myosin with MYL5 or alkali light chain increases filament velocity to intermediate rates, and the re-addition of both classes of light chains fully reinstates the original sliding pace.
-
Synonyms
Myosin light chain 5, Myosin regulatory light chain 5, Superfast myosin regulatory light chain 2, MYLC2, MyLC-2, MYL5.
-
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 MGSHMDQNRD GFIDKEDLKD TYASLGKTNV KDDELDAMLK EASGPINFTM FLNLFGEKLS GTDAEETILN AFKMLDPDGK GKINKEYIKR LLMSQADKMT AEEVDQMFQF ASIDVAGNLD YKALSYVITH GEEKEE.
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.