Search results
575 results found for “mitochondrial transcription factor”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
IGF1 Gilthead SeabreamDescription:
IGF1 Gilthead Seabream Recombinant
Somatomedin C, IGF-I, IGFI.
Product # :
CYT-295Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.IGF-1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.More Info
-
Introduction
The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.
-
Synonyms
Somatomedin C, IGF-I, IGFI.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK
-
Background
What is the molecular weight/Mw of IGF1 GILTHEAD SEABREAM Protein?
IGF1 GILTHEAD SEABREAM Protein has a total Mw of 7.54kDa.
What is the source or expression system of IGF1 GILTHEAD SEABREAM Protein?
Escherichia Coli.
What is the Purity of IGF1 GILTHEAD SEABREAM Protein?
IGF1 GILTHEAD SEABREAM Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of IGF1 GILTHEAD SEABREAM Protein?
Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.
What is the amino acid sequence of IGF1 GILTHEAD SEABREAM Protein?
MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK
What applications can IGF1 GILTHEAD SEABREAM Protein be used in?
IGF1 GILTHEAD SEABREAM Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for IGF1 GILTHEAD SEABREAM Protein?
The endotoxin level is minimal, IGF1 GILTHEAD SEABREAM Protein was purified using conventional chromatography techniques.
-
Protein content
Somatomedin C quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.60 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). 2. Analysis by RP-HPLC, using a calibrated solution of IGF1 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.
- View Data Sheet
Description:
Ornithine Aminotransferase Human Recombinant
DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.
Product # :
ENZ-472Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Ornithine Aminotransferase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 408 amino acids (33-439 a.a.) and having a molecular wieght of 45.2kDa.The Ornithine Aminotransferase is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Ornithine Aminotransferase protein solution contains 20mM Tris, pH-8, and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Ornithine Aminotransferase is a mitochondrial enzyme which is an important factor that converts arginine and ornithine into the major excitatory and inhibitory neurotransmitters glutamate and GABA. Ornithine Aminotransferase mutations result in a deficiency that cause the autosomal recessive eye disease Gyrate Atrophy.
-
Synonyms
DKFZp781A11155, HOGA, OATASE, Ornithine aminotransferase mitochondrial, Ornithine--oxo-acid aminotransferase, OAT, OKT, GACR.
-
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
MTVQGPPTSD DIFEREYKYG AHNYHPLPVA LERGKGIYLW DVEGRKYFDF LSSYSAVNQG HCHPKIVNAL KSQVDKLTLT SRAFYNNVLG EYEEYITKLF NYHKVLPMNT GVEAGETACK LARKWGYTVK GIQKYKAKIV AAGNFWGRT LSAISSSTDP TSYDGFGPFM PGFDIIPYND LPALERALQD PNVAAFMVEP IQGEAGVVVP DPGYLMGVRE LCTRHQVLFI ADEIQTGLAR TGRWLAVDYE NVRPDIVLLG KALSGGLYPV SAVLCDDDIM LTIKPGEHGS TYGGNPLGCR VAIAALEVLE EENLAENADK LGIILRNELM KLPSDVVTAV RGKGLLNAIV IKETKDWDAW KVCLRLRDNG LLAKPTHGDI IRFAPPLVIK EDELRESIEI INKTILSF.
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 :
GFRA3 HumanDescription:
GDNF Family Receptor Alpha 3 Human Recombinant
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.
Product # :
CYT-399Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
- sds-page
Description
GFRA3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (32-374a.a) and having a molecular mass of 40.7kDa.GFRA3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
GFRA3 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) 0.4M urea and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
-
Introduction
GDNF Family Receptor Alpha 3 (GFRA3) belongs to the GDNF receptor family. GFRA3 creates a signaling receptor complex with RET tyrosine kinase receptor and binds the ligand, artemin (ARTN).
-
Synonyms
GDNF Family Receptor Alpha3, GDNFR-alpha-3, GFR-alpha-3, GDNF Receptor Alpha-3, GDNFR3, GDNF Family Receptor Alpha-3, Glial Cell Line-Derived Neurotrophic Factor Receptor Alpha-3, GPI-Linked Receptor.
-
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
MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN
-
Background
What is the molecular weight/Mw of GFRA3 HUMAN Protein?
GFRA3 HUMAN Protein has a total Mw of 40.7kDa.
What is the source or expression system of GFRA3 HUMAN Protein?
Escherichia Coli.
What is the Purity of GFRA3 HUMAN Protein?
GFRA3 HUMAN Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of GFRA3 HUMAN Protein?
The biological functionality of GFRA3 HUMAN Protein will be determined in the future.
What is the amino acid sequence of GFRA3 HUMAN Protein?
MGSSHHHHHH SSGLVPRGSH MGSDPLPTES RLMNSCLQAR RKCQADPTCS AAYHHLDSCT SSISTPLPSE EPSVPADCLE AAQQLRNSSL IGCMCHRRMK NQVACLDIYW TVHRARSLGN YELDVSPYED TVTSKPWKMN LSKLNMLKPD SDLCLKFAML CTLNDKCDRL RKAYGEACSGPHCQRHVCLR QLLTFFEKAA EPHAQGLLLC PCAPNDRGCG ERRRNTIAPN CALPPVAPNC LELRRLCFSD PLCRSRLVDF QTHCHPMDIL GTCATEQSRC LRAYLGLIGT AMTPNFVSNV NTSVALSCTC RGSGNLQEEC EMLEGFFSHN PCLTEAIAAK MRFHSQLFSQ DWPHPTFAVMAHQNEN
What applications can GFRA3 HUMAN Protein be used in?
GFRA3 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GFRA3 HUMAN Protein?
The endotoxin level is minimal, GFRA3 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SIRT5 HumanDescription:
Sirtuin-5 Human Recombinant
Sirtuin 5, NAD-Dependent Lysine Demalonylase And Desuccinylase Sirtuin-5,Mitochondria, NAD-Dependent Protein Deacylase Sirtuin-5 Mitochondrial, Silent Mating Type Information Regulation 2 (S.Cerevisiae) Homolog 5, NAD-Dependent Deacetylase Sirtuin-5, Regulatory Protein SIR2 Homolog 5, SIR2-Like Protein 5, SIR2L5, Sirtuin Type 5, Sir2-Like 5, EC 3.5.1.-.
Product # :
PRO-1774Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SIRT5 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain topological domain containing 300 amino acids (34-310 a.a) and having a molecular mass of 32.5kDa. SIRT5 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SIRT5 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 30% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
SIRT5 belongs to the Sirtuin family of proteins, homologs to the yeast Sir2 protein. Sirtuin family members hold a sirtuin core domain and grouped into four classes. The protein encoded by this gene is included in class III of the sirtuin family. Human sirtuins functions were not yet determined; still, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies propose that human sirtuin could operate as intracellular regulatory protein with mono-ADP-ribosyltransferase activity.
-
Synonyms
Sirtuin 5, NAD-Dependent Lysine Demalonylase And Desuccinylase Sirtuin-5,Mitochondria, NAD-Dependent Protein Deacylase Sirtuin-5 Mitochondrial, Silent Mating Type Information Regulation 2 (S.Cerevisiae) Homolog 5, NAD-Dependent Deacetylase Sirtuin-5, Regulatory Protein SIR2 Homolog 5, SIR2-Like Protein 5, SIR2L5, Sirtuin Type 5, Sir2-Like 5, 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
MGSSHHHHHH SSGLVPRGSH MGSARPSSSM ADFRKFFAKA KHIVIISGAG VSAESGVPTF RGAGGYWRKW QAQDLATPLA FAHNPSRVWE FYHYRREVMG SKEPNAGHRA IAECETRLGK QGRRVVVITQ NIDELHRKAG TKNLLEIHGS LFKTRCTSCG VVAENYKSPI CPALSGKGAP EPGTQDASIP VEKLPRCEEA GCGGLLRPHV VWFGENLDPA ILEEVDRELA HCDLCLVVGT SSVVYPAAMF APQVAARGVP VAEFNTETTP ATNRFRFHFQ GPCGTTLPEA LACHENETVS
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 :
Leptin tA MouseDescription:
Leptin Antagonist Triple Mutant Mouse Recombinant
Product # :
CYT-354Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Leptin Antagonist Triple Mutant Mouse Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, LEP was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Mouse Recombinant was purified by proprietary chromatographic techniques.
Source
Escherichia coli.
Formulation
The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
ProSpec’s Leptin Antagonist Triple Mutant Mouse Recombinant 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 Mouse Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Leptin mutant mg/ml and up to 2 mM and filter sterilization LEP 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 Mouse Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with 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 quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.201 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.
- View Data Sheet
Name :
SCO2 HumanDescription:
SCO Cytochrome Oxidase Deficient Homolog 2 Human Recombinant
SCO1L, SCO Cytochrome Oxidase Deficient Homolog 2 (yeast), Protein SCO2 Homolog-Mitochondrial, MGC125823, MGC125825.
Product # :
PRO-054Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SCO2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (42-266a.a.) and having a molecular mass of 27.4kDa.SCO2 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SCO2 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0) 2mM DTT, 200mM NaCl and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
SCO2 protein is a member of the SCO1/2 family. SCO1 and SCO2 proteins are found on the inner membrane of the mitochondria and takes a vital part copper insertion or transport to the active site of cytochrome c oxidase (COX). Flaws in SCO2 are the reason for deadly infantile cardioencephalomyopathy with cytochrome c oxidase deficiency (FIC) which is characterized by hypertrophic cardiomyopathy, lactic acidosis, and gliosis. Heart and skeletal muscle display declines in cytochrome c oxidase (COX) activity, while liver and fibroblasts show mild COX deficiencies.
-
Synonyms
SCO1L, SCO Cytochrome Oxidase Deficient Homolog 2 (yeast), Protein SCO2 Homolog-Mitochondrial, MGC125823, MGC125825.
-
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.Please avoid freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGPAETGGQG QPQGPGLRTR LLITGLFGAG LGGAWLALRA EKERLQQQKR TEALRQAAVG QGDFHLLDHR GRARCKADFR GQWVLMYFGF THCPDICPDE LEKLVQVVRQ LEAEPGLPPV QPVFITVDPE RDDVEAMARY VQDFHPRLLG LTGSTKQVAQ ASHSYRVYYN AGPKDEDQDY IVDHSIAIYL LNPDGLFTDY YGRSRSAEQI SDSVRRHMAA FRSVLS
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 :
LMX1B HumanDescription:
LIM Homeobox Transcription Factor 1, Beta Human Recombinant
LIM homeobox transcription factor 1, beta, LMX1.2, NPS1, LIM/homeobox protein 1.2, LIM/homeobox protein LMX1B, LMX1B.
Product # :
PRO-1999Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
LMX1B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (1-395a.a) and having a molecular mass of 46.5kDa. LMX1B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LMX1B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
LIM Homeobox Transcription Factor 1, Beta (LMX1B) is a part of LIM-homeodomain family of proteins which consists of 2 N-terminal zinc-binding LIM domains, 1 homeodomain, and a C-terminal glutamine-rich domain. LMX1B plays a role as a transcription factor and is necessary for the specification of dorsal limb fate at the zeugopodal and autopodal levels. Mutations in LMX1B are associated with nailpatella syndrome.
-
Synonyms
LIM homeobox transcription factor 1, beta, LMX1.2, NPS1, LIM/homeobox protein 1.2, LIM/homeobox protein LMX1B, LMX1B.
-
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 MGSMDIATGP ESLERCFPRG QTDCAKMLDG IKMEEHALRP GPATLGVLLG SDCPHPAVCE GCQRPISDRF LMRVNESSWH EECLQCAACQ QALTTSCYFR DRKLYCKQDY QQLFAAKCSG CMEKIAPTEF VMRALECVYH LGCFCCCVCE RQLRKGDEFV LKEGQLLCKG DYEKEKDLLS SVSPDESDSV KSEDEDGDMK PAKGQGSQSK GSGDDGKDPR RPKRPRTILT TQQRRAFKAS FEVSSKPCRK VRETLAAETG LSVRVVQVWF QNQRAKMKKL ARRHQQQQEQ QNSQRLGQEV LSSRMEGMMA SYTPLAPPQQ QIVAMEQSPY GSSDPFQQGL TPPQMPGNDS IFHDIDSDTS LTSLSDCFLG SSDVGSLQAR VGNPIDRLYS MQSSYFAS.
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 :
FAS AntibodyDescription:
FAS Blocking/Activating antibody (CD95), Mouse anti Human
FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95, Tumor necrosis factor receptor superfamily member 6 TNR6, APT1, FAS1, TNFRSF6.
Product # :
ANT-204Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- formulation
- More Info
Formulation
1 mg/ml in PBS (after reconstitution).
More Info
-
Introduction
The Fas receptor (CD95) mediates apoptotic signaling by Fas-ligand expressed on the surface of other cells. The Fas-FasL interaction plays an important role in the immune system and lack of this system leads to autoimmunity, indicating that Fas-mediated apoptosis removes self-reactive lymphocytes. Fas signaling is also involved in immune surveillance to remove transformed cells and virus infected cells. Binding of FAS to oligimerized FasL on another cell activates apoptotic signaling through a cytoplasmic domain termed the death domain that interacts with signaling adaptors including FAF, FADD and DAX to activate the caspase proteolytic cascade. Caspase-8 and caspase-10 are first activated, to then cleave and activate downstream caspases, and a variety of cellular substrates that lead to cell death. Caspases cleave nuclear lamins, causing the nucleus to break down and lose its normal structure and another caspase substrate is DFF, inducing cleavage and degradation of the genome. Other caspase substrates are involved in cytoskeletal structure, cell cycle regulation and signaling pathways. Activation of JNK kinase, activation of Jun, and production of ceramide may also play roles in Fas-mediated apoptosis. Activation of fas-mediated apoptosis is opposed by I-FLICE and FAP. Viruses and tumors may escape immune surveillance in part through suppression of fas-mediated apoptosis using similar mechanisms.
-
Synonyms
FASLG receptor, Apoptosis-mediating surface antigen FAS, Apo-1 antigen, CD95, Tumor necrosis factor receptor superfamily member 6 TNR6, APT1, FAS1, TNFRSF6.
-
Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
-
Immunogen
Recombinant Human FAS.
-
Ig Subclass
mouse IgG1.
-
Clone
NYRhFAS.
-
Note
This antibody is a BLOCKING antibody when in soluble form and will block FAS-mediated apoptosis. It will ACTIVATE FAS-mediated killing when immobilized.
-
Titer
By direct ELISA, 1:10,000 dilution will yield 0.5 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
-
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
In lyophilized form, for long periods, store at 4°C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20°C.
-
Purification Method
Protein-A column.
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 :
Frataxin HumanDescription:
Frataxin Human Recombinant
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
Product # :
PRO-761Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Frataxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids (42-210 a.a.) and having a molecular mass of 21.1 kDa. The Frataxin is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Frataxin solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 0.1M NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Frataxin is a mitochondrial iron binding protein that is part of the FRATAXIN family. Frataxin functions in regulating mitochondrial iron transport and respiration. The expansion of intronic trinucleotide repeat GAA results in Friedreich ataxia. Frataxin plays a role in iron homeostasis. Frataxin is an anti-apoptotic protein which prevents mitochondrial damage and reactive oxygen species (ROS) production.
-
Synonyms
FXN, Friedreich ataxia protein, Frataxin mitochondrial, FRDA, X25, FA, CyaY, FARR, MGC57199, Frataxin.
-
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 MLRTDIDATC TPRRASSNQR GLNQIWNVKK QSVYLMNLRK SGTLGHPGSL DETTYERLAE ETLDSLAEFF EDLADKPYTF EDYDVSFGSG VLTVKLGGDL GTYVINKQTP NKQIWLSSPS SGPKRYDWTG KNWVYSHDGV SLHELLAAEL TKALKTKLDL SSLAYSGKDA.
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 :
EGF MouseDescription:
Epidermal Growth Factor Mouse
Urogastrone, URG, EGF.
Product # :
CYT-554Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Epidermal Growth Factor Mouse purified from submaxillary gland is a single, glycosylated, polypeptide chain having a molecular mass of 6.1 kDa.The EGF is purified by proprietary chromatographic techniques.
Source
Mouse Submaxillary Gland.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution containing 0.01M sodium acetate buffer.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity is measured in a proliferation assay using BALB/MK cells.More Info
-
Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. -
Synonyms
Urogastrone, URG, EGF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Epidermal Growth Factor Mouse although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF 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 Epidermal Growth Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Background
Illuminating Novel Avenues: Epidermal Growth Factor Mouse Variant in Cellular Dynamics and Therapeutic Prospects
Abstract:
This research paper delves into unexplored dimensions of the Epidermal Growth Factor Mouse Variant (EGF-M), unraveling its intricate molecular attributes, signaling cascades, and therapeutic implications. Employing advanced methodologies encompassing transgenic models, cellular assays, and bioinformatics, this study unveils the nuanced cellular responses elicited by EGF-M. The findings underscore its potential as a therapeutic target for regenerative medicine and cancer interventions.
Introduction:
Epidermal Growth Factor (EGF) orchestrates pivotal cellular processes. This paper charts a new course, focusing on the Epidermal Growth Factor Mouse Variant (EGF-M), exploring its distinct molecular properties and therapeutic applications.
Molecular Insights and Receptor Binding:
EGF-M's interaction with the epidermal growth factor receptor (EGFR) initiates a cascade of intracellular events. Molecular dynamics simulations and binding studies decipher the nuances of this interaction, shedding light on structural motifs that drive receptor activation and downstream signaling.
Cellular Signaling and Functional Responses:
EGF-M engages canonical and non-canonical signaling pathways, including the mitogen-activated protein kinase (MAPK) pathway and phosphoinositide 3-kinase (PI3K)/Akt pathway. High-resolution microscopy and phosphoproteomics unveil spatiotemporal dynamics, revealing how EGF-M orchestrates cell proliferation, migration, and survival.
Transgenic Mouse Models and In Vivo Implications:
In transgenic mouse models, EGF-M's impact on tissue regeneration becomes evident. Tailored wound healing assays demonstrate accelerated re-epithelialization and granulation tissue formation, affirming its potential in regenerative medicine. Furthermore, xenograft studies suggest its role in modulating tumor microenvironments, offering prospects for cancer therapy.
Bioinformatics in EGF-M Interactions:
Advanced bioinformatics analyses deepen our understanding of EGF-M's cellular interactions. Molecular docking simulations predict potential binding partners and off-target effects, enhancing our comprehension of its biological scope.
Therapeutic Implications and Future Directions:
EGF-M's distinctive attributes open doors for therapeutic innovation. Exploiting its regenerative potential, it holds promise for chronic wound management and tissue engineering. Moreover, targeted interventions exploiting its role in cancer microenvironments might revolutionize oncology treatments.
Challenges and Prospects:
Despite promising strides, challenges linger, including deciphering cross-talk between signaling pathways. Future research should focus on refining delivery methods and optimizing dosage regimens to harness EGF-M's therapeutic potential.
Conclusion:
In a synthesis of intricate molecular insights and transformative therapeutic avenues, Epidermal Growth Factor Mouse Variant emerges as a captivating subject. Its distinctive binding mechanisms and multifaceted cellular orchestration spotlight its potential as a regenerative agent and a cancer therapeutic, propelling medical science into a new era.
What is the molecular weight/Mw of EGF Protein?
EGF Protein has a total Mw of 6.1Da.
What is the source or expression system of EGF Protein?
Mouse Submaxillary Gland.
What is the Purity of EGF Protein?
EGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of EGF Protein?
The biological activity is measured in a proliferation assay using BALB/MK cells.
What is the amino acid sequence of EGF Protein?
EGF Protein is composed from 53 amino acids.
What applications can EGF Protein be used in?
EGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for EGF Protein?
The endotoxin level is minimal, EGF 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 :
CEBP Gamma HumanDescription:
CCAAT/enhancer binding protein C/EBP Gamma Recombinant Human
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-1.
Product # :
PRO-434Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CEBP-g Recombinant Human His-Tag fusion protein produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 146 (aa 39-147) and having a molecular mass of 16.5 kDa. The DNA binding domain of CEBP-g was purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein contains 20mM Tris-HCl pH7.5, 0.1M NaCl and 5mM b-Mercaptoethanol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CCAAT/enhancer binding protein(C/EBP) g is a family of transcription factors all contain a highly conserved, basic-leucine zipper domain at the C-terminus that is involved in dimerization and DNA binding. C/EBP family of transcription factors regulates viral and cellular CCAAT/enhancer element-mediated transcription. C/EBP family consist of several related proteins, C/EBP a,b,g,d, that form homodimers and/or form heterodimers with each other. C/EBP proteins contain the bZIP region, which is characterized by two motifs in the C-terminal half of the protein; a basic region involved in DNA binding and a leucine zipper motif involved in dimerization. C/EBP g may cooperate with Fos to bind PRE- enhancer elements.
-
Synonyms
CCAAT/enhancer-binding protein gamma, C/EBP gamma, CEBPG, GPE1BP, IG/EBP-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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMPGG GGKAVAPSKQ SKKSSPMDRN SDEYRQRRER NNMAVKKSRL KSKQKAQDTL QRVNQLKEEN ERLEAKIKLL TKELSVLKDL FLEHAHNLAD NVQSISTENT TADGDN.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GroES Human, HisDescription:
GroES (HSP10) Human Recombinant, His Tag
CPN10, GROES, HSP10, HSPE1, Chaperonin-10, 10 kDa heat shock protein mitochondrial, 10 kDa chaperonin, Early-pregnancy factor, EPF.
Product # :
HSP-040Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
GroES His Protein is 12.0 kDa protein containing 111 amino acid residues of the GroES Human and the 10 aa N-Terminal His-tag.
Source
E. coli
Formulation
GroES His Human was filtered (0.4µm) and lyophilized from 0.5 mg/ml supplied in 0.05M phosphate buffer, 0.075 M NaCl, pH 7.4.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
HSP10 is part of the molecular chaperons, that are crucial for thir efficient folding of proteins in normal as well as stress conditions. GroES function is to bind to HSP60 in the presence of ATP, thus causing a change in the HSP60 conformation & enclosing the protein substrate within the complex. ATP hydrolysis by chaperonin-60 which destabilizes the HSP10-HSP60 complex, thereby allowing it to dissociate and secrete the substrate protein. GroES having the NCBI accession number of NP_002148 was purified by using conventional chromatography techniques.
-
Synonyms
CPN10, GROES, HSP10, HSPE1, Chaperonin-10, 10 kDa heat shock protein mitochondrial, 10 kDa chaperonin, Early-pregnancy factor, EPF.
-
Stability
Store lyophilized GroES His at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted GroES His can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
-
Amino Acid Sequence
MKHHHHHHAS AGQAFRKFLP LFDRVLVERS AAETVTKGGI MLPEKSQGKV LQATVVAVGS GSKGKGGEIQ PVSVKVGDKV LLPEYGGTKV VLDDKDYFLF RDGDILGKYV D.
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 :
IL 22 RatDescription:
Interleukin-22 Rat Recombinant
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Product # :
CYT-173Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IL-22 Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.6kDa.The IL22 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity is measured by its ability to induce IL-10 secretion in COLO 205 (human colon carcinoma cells). The expected ED50 for this effect is 0.15-0.75ng/ml.More Info
-
Introduction
IL-22 is a member of the IL-10 family of regulatory cytokines.Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10R-beta/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family.
-
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Interleukin-22 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 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 Interleukin -22 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
LPINSQCKLE AANFQQPYIV NRTFMLAKEA SLADNNTDVR LIGEELFRGV KAKDQCYLMK QVLNFTLEDV LLPQSDRFQP YMQEVVPFLT KLSIHLSPCH ISGDDQNIQK NVRQLKETVQ KLGESGEIKA IGELDLLFMS LRNACV.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
FGF4 HumanDescription:
Fibroblast Growth Factor-4 Human Recombinant
HBGF4, FGF-4, FGF4, KFGF, HSTF1.
Product # :
CYT-312Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
FGF4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 182 amino acids and having a molecular mass of 19.8kDa. The FGF4 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The FGF4 protein was lyophilized with 20mM sodium phosphate and 500mM NaCl pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.
More Info
-
Introduction
FGF4 holds s comprehensive mitogenic and cell survival activities and takes part in a range of biological processes including embryonic development, cell growth, morphogenesis, tissue repair, tumor growth and invasion. FGF4 possess oncogenic transforming activity. FGF4 and FGF3, oncogenic growth factors are localized on chromosome 11. Co-amplification of both factors was found in several kinds of human tumors. FGF4 functions in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway.
-
Synonyms
HBGF4, FGF-4, FGF4, KFGF, HSTF1.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FGF4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF-4 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized FGF4 Human Recombinant sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.
-
Background
What is the molecular weight/Mw of FGF4 HUMAN Protein?
FGF4 HUMAN Protein has a total Mw of 19.8kDa.
What is the source or expression system of FGF4 HUMAN Protein?
Escherichia Coli.
What is the Purity of FGF4 HUMAN Protein?
FGF4 HUMAN Protein is > 95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF4 HUMAN Protein?
The ED50 as determined by NR6R-3T3 Proliferation is 0.54ng/ml, corresponding to a specific activity of 1.8X106 units/mg.
What is the amino acid sequence of FGF4 HUMAN Protein?
MAPTAPNGTL EAELERRWES LVALSLARLP VAAQPKEAAV QSGAGDYLLG IKRLRRLYCN VGIGFHLQAL PDGRIGGAHA DTRDSLLELS PVERGVVSIF GVASRFFVAM SSKGKLYGSP FFTDECTFKE ILLPNNYNAY ESYKYPGMFI ALSKNGKTKK GNRVSPTMKV THFLPRL.
What applications can FGF4 HUMAN Protein be used in?
FGF4 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF4 HUMAN Protein?
The endotoxin level is minimal, FGF4 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
OSM MouseDescription:
Oncostatin-M Mouse Recombinant
Oncostatin-M, OSM, OncoM.
Product # :
CYT-168Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
OSM Mouse Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids and having a molecular mass of 20.4kDa.The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of NIH-3T3 mouse embryonic fibroblast cells is < 1 ng/ml, corresponding to a specific activity of > 1.0×106 units/mg.More Info
-
Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
-
Synonyms
Oncostatin-M, OSM, OncoM.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
NRGCSNSSSQ LLSQLQNQAN LTGNTESLLE PYIRLQNLNT PDLRAACTQH SVAFPSEDTL RQLSKPHFLS TVYTTLDRVL YQLDALRQKF LKTPAFPKLD SARHNILGIR NNVFCMARLL NHSLEIPEPT QTDSGASRST TTPDVFNTKI GSCGFLWGYH RFMGSVGRVF REWDDGSTRS R.
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 :
LGALS8 Human, HisDescription:
Galectin-8 Human Recombinant, His Tag
Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 1.
Product # :
CYT-727Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- SDS-PAGE
Description
LGALS8 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-317 a.a.) and having a molecular mass of 37.9 kDa. The LGALS8 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Galectin-8 His tag 0.5mg/ml protein solution contains 20mM Tris-HCl pH-8, 0.1M NaCl, 10% glycerol & 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.SDS-PAGE
More Info
-
Introduction
LGALS8 is a prostate-specific antigen that is solely overexpressed in malignant tumors and thus is a supplementary specific identifier of malignancies. LGALS8 is part of the galectin gene family which facilitates both cell-cell and cell matrix interactions in a method parallel to the selectin subgroup of C-type lectins.
-
Synonyms
Gal-8, PCTA1, Po66-CBP, Prostate carcinoma tumor antigen 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 MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW. -
Background
What is the molecular weight/Mw of LGALS8 HUMAN, HIS Protein?
LGALS8 HUMAN, HIS Protein has a total Mw of 37.9kDa.
What is the source or expression system of LGALS8 HUMAN, HIS Protein?
Escherichia Coli.
What is the Purity of LGALS8 HUMAN, HIS Protein?
LGALS8 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of LGALS8 HUMAN, HIS Protein?
The ED50 for this effect is 5–10ug/ml. Measured by its ability to agglutinate human red blood cells corresponding to a specific activity of 100-200IU/mg.What is the amino acid
sequence of LGALS8 HUMAN, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MMLSLNNLQN IIYNPVIPFV GTIPDQLDPG TLIVIRGHVP SDADRFQVDL QNGSSMKPRA DVAFHFNPRF
KRAGCIVCNT LINEKWGREE ITYDTPFKRE KSFEIVIMVL KDKFQVAVNG KHTLLYGHRI GPEKIDTLGI YGKVNIHSIG FSFSSDLQST
QASSLELTEI SRENVPKSGT PQLRLPFAAR LNTPMGPGRT VVVKGEVNAN AKSFNVDLLA GKSKDIALHL NPRLNIKAFV RNSFLQESWG
EEERNITSFP FSPGMYFEMI IYCDVREFKV AVNGVHSLEY KHRFKELSSI DTLEINGDIH LLEVRSW.
What applications can LGALS8 HUMAN, HIS Protein be used in?
LGALS8 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for LGALS8 HUMAN, HIS Protein?
The endotoxin level is minimal, LGALS8 HUMAN, HIS Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ACADM HumanDescription:
Acyl-Coenzyme A Dehydrogenase, C-4 to C-12 Human Recombinant
ACADM, ACAD1, CAD, MCADH, MCAD, EC=1.3.99.3, Medium-chain specific acyl-CoA dehydrogenase, mitochondrial, FLJ18227, FLJ93013, FLJ99884.
Product # :
ENZ-529Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ACADM Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 417 amino acids (26-421 a.a.) and having a molecular mass of 45.9 kDa. The ACADM is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The ACADM (0.5mg/ml) protein solution containing 20mM Tris-HCl pH-7.5, 0.1M NaCl & 20% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
ACADM enzyme is essential for the degradation a certain group of fats called medium-chain fatty acids. ACADM is essential for converting specific fatty acids to energy, mainly during fasting periods. ACADM functions in mitochondria, the energy-producing centers within cells. ACADM is localized in the mitochondria of numerous tissue types, predominantly the liver.
-
Synonyms
ACADM, ACAD1, CAD, MCADH, MCAD, EC=1.3.99.3, Medium-chain specific acyl-CoA dehydrogenase, mitochondrial, FLJ18227, FLJ93013, FLJ99884.
-
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 MKANRQREPG LGFSFEFTEQ QKEFQATARK FAREEIIPVA AEYDKTGEYP VPLIRRAWEL GLMNTHIPEN CGGLGLGTFD ACLISEELAY GCTGVQTAIE GNSLGQMPII IAGNDQQKKK YLGRMTEEPL MCAYCVTEPG AGSDVAGIKT KAEKKGDEYI INGQKMWITN GGKANWYFLL ARSDPDPKAP ANKAFTGFIV EADTPGIQIG RKELNMGQRC SDTRGIVFED VKVPKENVLI GDGAGFKVAM GAFDKTRPVV AAGAVGLAQR ALDEATKYAL ERKTFGKLLV EHQAISFMLA EMAMKVELAR MSYQRAAWEV DSGRRNTYYA SIAKAFAGDI ANQLATDAVQ ILGGNGFNTE YPVEKLMRDA KIYQIYEGTS QIQRLIVARE HIDKYKN.
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 21 RatDescription:
Fibroblast Growth Factor-21 Rat Recombinant
Fibroblast growth factor 21, FGF-21.
Product # :
CYT-130Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
FGF 21 Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The FGF 21 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 determined by a cell proliferation assay using murine NIH/3T3 cells is less than 700 ng/ml, corresponding to a specific activity of > 1.4 × 1000 IU/mg in the presence of 5µg/ml of rMuKlotho-beta.
More Info
-
Introduction
The FGFs are a family of more than 20 small (~17–26 kDa) secreted peptides. The initial characterization of these proteins focused on their ability to stimulate fibroblast proliferation. This mitogenic activity was mediated through FGF receptors (FGFRs) 1, 2, or 3. A fourth closely related tyrosine kinase receptor (FGFR4) was able to bind the FGFs but did not lead to a mitogenic response.
FGFs modulate cellular activity via at least 5 distinct subfamilies of high-affinity FGF receptors (FGFRs): FGFR-1, -2, -3, and -4, all with intrinsic tyrosine kinase activity and, except for FGFR-4, multiple splice isoforms, and FGFR-5, which lacks an intracellular kinase domain. There is growing evidence that FGFRs can be important for regulation of glucose and lipid homeostasis. The overexpression of a dominant negative form of FGFR-1 in cells leads to diabetes in mice, which thus implies that proper FGF signaling is required for normal ? cell function and glycemia maintenance. FGFR-2 appears to be a key molecule during pancreatic development. Moreover, FGFR-4 has been implicated in cholesterol metabolism and bile acid synthesis.
FGF-19, has been shown to cause resistance to diet-induced obesity and desensitization and to improve glucose, and lipid profiles in diabetic rodents. Since these effects, at least in part, are mediated through the observed changes in metabolic rates, FGF-19 can be considered as a regulator of energy expenditure.
FGF-21 is preferentially expressed in liver, but an exact knowledge of FGF-21 bioactivity and its mode of action have been lacking to date. FGF-21 is a potent activator of glucose uptake on adipocytes, protects animals from diet-induced obesity when overexpressed in transgenic mice, and lowers blood glucose and triglyceride levels when therapeutically administered to diabetic rodents. -
Synonyms
Fibroblast growth factor 21, FGF-21.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized FGF 21 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF 21 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 FGF 21 Rat Recombinant in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
AYPISDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGTAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GTLYGSPHFD PEACSFRELL LKDGYNVYQS EAHGLPLRLP QKDSQDPATR GPVRFLPMPG LPHEPQEQPG VLPPEPPDVG SSDPLSMVEP LQGRSPSYAS
-
Background
What is the molecular weight/Mw of FGF21-RAT Protein?
FGF21-RAT Protein has a total Mw of 19.7kDa.
What is the source or expression system of FGF21-RAT Protein?
Escherichia Coli.
What is the Purity of FGF21-RAT Protein?
FGF21-RAT Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FGF21-RAT Protein?
The ED50 determined by a cell proliferation assay using murine NIH/3T3 cells is less than 700 ng/ml, corresponding to a specific activity of > 1.4 × 1000 IU/mg in the presence of 5µg/ml of rMuKlotho-beta.
What is the amino acid sequence of FGF21-RAT Protein?
AYPISDSSPL LQFGGQVRQR YLYTDDDQDT EAHLEIREDG TVVGTAHRSP ESLLELKALK PGVIQILGVK ASRFLCQQPD GTLYGSPHFD PEACSFRELL LKDGYNVYQS EAHGLPLRLP QKDSQDPATR GPVRFLPMPG LPHEPQEQPG VLPPEPPDVG SSDPLSMVEP LQGRSPSYAS
What applications can FGF21-RAT Protein be used in?
FGF21-RAT Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FGF21-RAT Protein?
The endotoxin level is minimal, FGF21-RAT Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
UQCRC1 HumanDescription:
Ubiquinol-Cytochrome C Reductase Core Protein I Human Recombinant
D3S3191, QCR1, UQCR1, Cytochrome b-c1 complex subunit 1, mitochondrial, Complex III subunit 1, Core protein I, Ubiquinol-cytochrome-c reductase complex core protein 1.
Product # :
PRO-1894Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
UQCRC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 471 amino acids (35-480 a.a) and having a molecular mass of 51.8kDa.UQCRC1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
UQCRC1protein 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.
More Info
-
Introduction
Ubiquinol-Cytochrome C Reductase Core Protein I (UQCRC1) is a member of the peptidase M16 family,UQCRC1/QCR1 subfamily. UQCRC1 is a part of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is component of the mitochondrial respiratory chain. UQCRC1 can mediate formation of the complex between cytochromes c and c1.
-
Synonyms
D3S3191, QCR1, UQCR1, Cytochrome b-c1 complex subunit 1, mitochondrial, Complex III subunit 1, Core protein I, Ubiquinol-cytochrome-c reductase complex core protein 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).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFTATFA QALQFVPETQ VSLLDNGLRV ASEQSSQPTC TVGVWIDVGS RFETEKNNGA GYFLEHLAFK GTKNRPGSAL EKEVESMGAH LNAYSTREHT AYYIKALSKD LPKAVELLGD IVQNCSLEDS QIEKERDVIL REMQENDASM RDVVFNYLHA TAFQGTPLAQ AVEGPSENVR KLSRADLTEY LSTHYKAPRM VLAAAGGVEH QQLLDLAQKH LGGIPWTYAE DAVPTLTPCR FTGSEIRHRD DALPFAHVAI AVEGPGWASP DNVALQVANA IIGHYDCTYG GGVHLSSPLA SGAVANKLCQ SFQTFSICYA ETGLLGAHFV CDRMKIDDMM FVLQGQWMRL CTSATESEVA RGKNILRNAL VSHLDGTTPV CEDIGRSLLT YGRRIPLAEW ESRIAEVDAS VVREICSKYI YDQCPAVAGY GPIEQLPDYN RIRSGMFWLR F.
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 :
GCSF MonkeyDescription:
Granulocyte Colony Stimulating Factor Recombinant Rhesus Macaque
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
Product # :
CYT-1121Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Granulocyte Colony Stimulating Rhesus Macaque Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 174 amino acids and having a molecular mass of approximately 18.9kDa.GCSF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.
More Info
-
Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. 3 transcript variants encoding 3 different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that take part in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
-
Synonyms
CSF3, MGI-1G, GM-CSF beta, Pluripoietin, G-CSF, GCSF.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Granulocyte Colony Stimulating Rhesus Macaque 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 Granulocyte Colony Stimulating Rhesus Macaque in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.
-
Background
What is the molecular weight/Mw of GCSF MONKEY Protein?
GCSF MONKEY Protein has a total Mw of 18.9kDa.
What is the source or expression system of GCSF MONKEY Protein?
Escherichia Coli.
What is the Purity of GCSF MONKEY Protein?
GCSF MONKEY Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of GCSF MONKEY Protein?
The ED50 as determined by a cell proliferation assay using murine NFS-60 cells is < 0.05 ng/ml, corresponding to a specific activity of > 2.0 × 107 IU/mg.
What is the amino acid sequence of GCSF MONKEY Protein?
TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL RHSLGIPWAP LSSCPSQALQ LTGCLSQLHS SLFLYQGLLQ ALEGISPELS PTLDTLQLDI ADFATTIWQQ MEDLGMAPAL QPTQGAMPAF TSAFQRRAGG VLVASHLQRF LELAYRVLRH LAQS.
What applications can GCSF MONKEY Protein be used in?
GCSF MONKEY Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for GCSF MONKEY Protein?
The endotoxin level is minimal, GCSF MONKEY 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 :
M CSF Human, HisDescription:
Macrophage Colony Stimulating Factor Human Recombinant, His Tag
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
Product # :
CYT-695Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Macrophage Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 179 amino acids (33-190 a.a.) and having a total molecular mass of 20.7 kDa.MCSF is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MCSF protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT & 10% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Granulocyte/Macrophage Colony-Stimulating Factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. CSF-1 induces cells of the monocyte/macrophage lineage. It plays a role in immunological defenses, bone metabolism, lipoproteins clearance, fertility and pregnancy.
-
Synonyms
CSF-1, Lanimostim, MCSF, MGC31930, M-CSF.
-
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 MEEVSEYCSH MIGSGHLQSL QRLIDSQMET SCQITFEFVD QEQLKDPVCY LKKAFLLVQD IMEDTMRFRD NTPNAIAIVQ LQELSLRLKS CFTKDYEEHD KACVRTFYET PLQLLEKVKN VFNETKNLLD KDWNIFSKNC NNSFAECSSQ DVVTKPDCN.
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 :
IL 11 Human, PichiaDescription:
Interleukin-11 Human Recombinant, Pichia
Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.
Product # :
CYT-013Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
IL11 was Lyophilized from a 0.2 µm filtered concentrated solution of 20mM PB, pH7.2 and 2% Glycine buffer.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng-0.8ng/ml, corresponding to a Specific Activity of greater than 1,000,000 IU/ mg.
More Info
-
Introduction
IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130). IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.
-
Synonyms
Interleukin-11, IL-11, Adipogenesis inhibitory factor, AGIF, Oprelvekin, IL11.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized IL11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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 Interleukin -11 in sterile 18MΩ-cm H2O 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 Gly-Pro-Pro-Pro-Gly.
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 :
OSR2 HumanDescription:
Odd-Skipped Related Transcription Factor 2 Human Recombinant
Odd-Skipped Related Transcription Factor 2 , Odd-Skipped Related 2 (Drosophila), Protein odd-skipped-related 2.
Product # :
PRO-2067Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
OSR2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 299 amino acids (1-276 a.a) and having a molecular mass of 33kDa. OSR2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
OSR2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
-
Introduction
Odd-Skipped Related Transcription Factor 2, also know as OSR2 belongs to the Odd C2H2-type zinc-finger protein family. OSR2 is a mammalian homolog of the Drosophila odd-skipped family of transcription factors.
-
Synonyms
Odd-Skipped Related Transcription Factor 2 , Odd-Skipped Related 2 (Drosophila), Protein odd-skipped-related 2.
-
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 MGSMGSKALP APIPLHPSLQ LTNYSFLQAV NTFPATVDHL QGLYGLSAVQ TMHMNHWTLG YPNVHEITRS TITEMAAAQG LVDARFPFPA LPFTTHLFHP KQGAIAHVLP ALHKDRPRFD FANLAVAATQ EDPPKMGDLS KLSPGLGSPI SGLSKLTPDR KPSRGRLPSK TKKEFICKFC GRHFTKSYNL LIHERTHTDE RPYTCDICHK AFRRQDHLRD HRYIHSKEKP FKCQECGKGF CQSRTLAVHK TLHMQTSSPT AASSAAKCSG ETVICGGTA.
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 :
CNTF MouseDescription:
Ciliary-Neurotrophic Factor Mouse Recombinant
HCNTF, CNTF, Ciliary Neurotrophic Factor.
Product # :
CYT-139Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Ciliary Neurotrophic Factor Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids and having a molecular mass of 22.6kDa. The CNTF 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:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of TF-1 cells is less than 35ng/ml, corresponding to a Specific Activity of 3.0×104 IU/mg.More Info
-
Introduction
CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy. -
Synonyms
HCNTF, CNTF, Ciliary Neurotrophic Factor.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF 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 CNTF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MAFAEQSPLT LHRRDLCSRS IWLARKIRSD LTALMESYVK HQGLNKNISL DSVDGVPVAS TDRWSEMTEA ERLQENLQAY RTFQGMLTKL LEDQRVHFTP TEGDFHQAIH TLTLQVSAFA YQLEELMALL EQKVPEKEAD GMPVTIGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRVIS SHHMGISAHE SHYGAKQM
-
Background
What is the molecular weight/Mw of CNTF Protein?
CNTF Protein has a total Mw of 22.6kDa.
What is the source or expression system of CNTF Protein?
Escherichia Coli.
What is the Purity of CNTF Protein?
CNTF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of CNTF Protein?
Fully biologically active when compared to standard. The ED50 as determined by the dose-dependant stimulation of TF-1 cells is less than 35ng/ml, corresponding to a Specific Activity of 3.0×104 IU/mg.
What is the amino acid sequence of CNTF Protein?
MAFAEQSPLT LHRRDLCSRS IWLARKIRSD LTALMESYVK HQGLNKNISL DSVDGVPVAS TDRWSEMTEA ERLQENLQAY RTFQGMLTKL LEDQRVHFTP TEGDFHQAIH TLTLQVSAFA YQLEELMALL EQKVPEKEAD GMPVTIGDGG LFEKKLWGLK VLQELSQWTV RSIHDLRVIS SHHMGISAHE SHYGAKQM
What applications can CNTF Protein be used in?
CNTF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CNTF Protein?
The endotoxin level is minimal, CNTF 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.