Search results
1000 results found for “decarboxylase”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
PKLR HumanDescription:
Pyruvate Kinase, Liver and RBC Human Recombinant
PK1, PKL, RPK, pyruvate kinase isozyme R/L, Red cell/liver pyruvate kinase, PKRL
Product # :
PKA-307Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
PKLR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 549 amino acids (47-574a.a.) and having a molecular wieght of 59.2kDa. The PKLR is fused to 21a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PKLR protein solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 1mM DTT 0.2M NaCl and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity: >0.1 unit/mg. One unit will form 1.0 umol of phospho(enol)pyruvate to pyruvate per minute at pH 7.5 at 37C.More Info
-
Introduction
PKLR is a pyruvate kinase which catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP. That is the rate-limiting step of glycolysis. PKLR gene encodes the L- and R-type isoenzymes through alternate splicing events controlled by different promoters. L-type isoform can also appear as a tetramer and is upregulated by glucose with implications in maturity-onset diabetes of the young.
-
Synonyms
PK1, PKL, RPK, pyruvate kinase isozyme R/L, Red cell/liver pyruvate kinase, PKRL
-
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 MLTQELGTAF FQQQQLPAAM ADTFLEHLCL LDIDSEPVAA RSTSIIATIG PASRSVERLK EMIKAGMNIA RLNFSHGSHE YHAESIANVR EAVESFAGSP LSYRPVAIAL DTKGPEIRTG ILQGGPESEV ELVKGSQVLV TVDPAFRTRG NANTVWVDYP NIVRVVPVGG RIYIDDGLIS LVVQKIGPEG LVTQVENGGV LGSRKGVNLP GAQVDLPGLS EQDVRDLRFG VEHGVDIVFA SFVRKASDVA AVRAALGPEG HGIKIISKIE NHEGVKRFDE ILEVSDGIMV ARGDLGIEIP AEKVFLAQKM MIGRCNLAGK PVVCATQMLE SMITKPRPTR AETSDVANAV LDGADCIMLS GETAKGNFPV EAVKMQHAIA REAEAAVYHR QLFEELRRAA PLSRDPTEVT AIGAVEAAFK CCAAAIIVLT TTGRSAQLLS RYRPRAAVIA VTRSAQAARQ VHLCRGVFPL LYREPPEAIW ADDVDRRVQF GIESGKLRGF LRVGDLVIVV TGWRPGSGYT NIMRVLSIS.
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 :
Benzonase Nuclease, 90%Description:
Benzonase Nuclease Serratia Marcescens Recombinant, 90%
Product # :
ENZ-1150Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Benzonase Nuclease Serratia Marcescens Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 30kDa with 2 essential disulfide bonds. Benzonase Nuclease is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Benzonase Nuclease solution contains 50% glycerol, 50 mM Tris-HCl pH 8.0, 20 mM NaCl and 2 mM MgCl2.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Serratia marcescens secretes an endonuclease that has exceptionally high specific activity to the medium that surrounds it. The Benzonase Nuclease is mainly used for elimination of nucleic acid contamination from purified proteins, downstream processing, reduction of viscosity etc. Nucleic acid contaminants are caused by nuclease released to the medium. The DNA is being destroyed by the release of the S. marcescens nuclease and it acts as the killer gene for the auto destruction of microorganisms.
-
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.
-
Specificity
Unspecific (DNA, RNA) attacks all nucleic acids (single strand, double strand, circular, supercoiled) with no apparent sequence preference. Final reaction product: 5’-mono-phosphate terminated oligonucleotides (3-5 bases). Protease Activity: Not detectable
-
Unit Definition
1U Benzonase Nuclease is defined as the amount of enzyme that causes a ΔA260 of 1 in 30 min, which corresponds to complete digestion of 37μg DNA. Standard reaction conditions are 1mg/ml sonicated DNA substrate in 50mM Tris-HCl pH 8.0, 0.1mg/ml BSA, 1mM MgCl2, incubated at 37°C.
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 :
ALPP Human, ActiveDescription:
Alkaline Phosphatase Placental Human Recombinant, BioActive
3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
Product # :
ENZ-1133Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
ALPP Human produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 494 amino acids (23-506 a.a.) and having a molecular mass of 53.9kDa. ALPP is expressed with a 10 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
ALPP protein solution (0.5mg/ml) containing Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,500unit/mg, and is defined as the amount of enzyme that hydrolyze 1.0nmole of pnitrophenyl phosphate (pNPP) per minute at pH 7.5 at 37C.
More Info
-
Introduction
Placental alkaline phosphatase also known as PLAP is a membranal siaglycoprotein enzyme typicallyfoundin high concentration in syncytiotrophoblasts in the placenta amid the 3th trimester of gestation. The expression of PLAP was at firstconsidered to be onlyin the term placenta, though, a human PLAP-like variant has been found,thathas more than 85% homology with PLAP itself. PLAP is expressed strictly in normal term placenta, endocervix & fallopian tube and in ovarian and proximal gastrointestinal tumors. It is also widely expressed in germ cell tumors and more recently found in seminomas.
-
Synonyms
3 ALPP, Alkaline phosphatase Regan isozyme, Placental alkaline phosphatase 1, PLAP-1, ALP, PLAP, Alkaline phosphatase placental type, EC 3.1.3.1, PLAP-1, Alkaline phosphatase Regan isozyme.
-
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
ADLMIIPVEE ENPDFWNREA AEALGAAKKL QPAQTAAKNL IIFLGDGMGV STVTAARILK GQKKDKLGPE LPLAMDRFPY VALSKTYNVD KHVPDSGATA TAYLCGVKGN FQTIGLSAAA RFNQCNTTRG NEVISVMNRA KKAGKSVGVV TTTRVQHASP AGTYAHTVNR NWYSDADVPA SARQEGCQDI ATQLISNMDI DVILGGGRKY MFRMGTPDPE YPDDYSQGGT RLDGKNLVQE WLAKRQGARY VWNRTELMQA SLDPSVTHLM GLFEPGDMKY EIHRDSTLDP SLMEMTEAAL RLLSRNPRGF FLFVEGGRID HGHHESRAYR ALTETIMFDD AIERAGQLTS EEDTLSLVTA DHSHVFSFGG YPLRGSSIFG LAPGKARDRK AYTVLLYGNG PGYVLKDGAR PDVTESESGS PEYRQQSAVP LDEETHAGED VAVFARGPQA HLVHGVQEQT FIAHVMAFAA CLEPYTACDL APPAGTTDHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
IMPA2 HumanDescription:
Inositol Monophosphatase 2 Human Recombinant
Inositol monophosphatase 2, IMP 2, IMPase 2, Inositol-1(or 4)-monophosphatase 2, Myo-inositol monophosphatase A2, IMPA2, IMP.18P.
Product # :
ENZ-070Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
IMPA2 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 308 amino acids (1-288 a.a.) and having a molecular mass of 33.5kDa. The IMPA2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The IMPA2 solution (0.25 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol and 2mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
IMPA2 is a member of the inositol monophosphatase family. IMPA2 catalyzes the dephosphoylration of inositol monophosphate and has a significant role in phosphatidylinositol signaling. IMPA2 can use the myo-inositol monophosphates, scylloinositol 1,4-diphosphate, glucose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates. IMPA2 is a pharmacological target for lithium Li(+) action in brain. IMPA2 is considered to have a role in schizophrenia and bipolar disorder.
-
Synonyms
Inositol monophosphatase 2, IMP 2, IMPase 2, Inositol-1(or 4)-monophosphatase 2, Myo-inositol monophosphatase A2, IMPA2, IMP.18P.
-
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 MKPSGEDQAA LAAGPWEECF QAAVQLALRA GQIIRKALTE EKRVSTKTSA ADLVTETDHL VEDLIISELR ERFPSHRFIA EEAAASGAKC VLTHSPTWII DPIDGTCNFV HRFPTVAVSI GFAVRQELEF GVIYHCTEER LYTGRRGRGA FCNGQRLRVS GETDLSKALV LTEIGPKRDP ATLKLFLSNM ERLLHAKAHG VRVIGSSTLA LCHLASGAAD AYYQFGLHCW DLAAATVIIR EAGGIVIDTS GGPLDLMACR VVAASTREMA MLIAQALQTI NYGRDDEK.
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 :
KDSR HumanDescription:
3-Ketodihydrosphingosine Reductase Human Recombinant
3-ketodihydrosphingosine reductase, KDS reductase, 3-dehydrosphinganine reductase, Follicular variant translocation protein 1, FVT-1, KDSR, FVT1, DHSR, SDR35C1, FLJ36555, FLJ92680.
Product # :
ENZ-092Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
KDSR Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 266 amino acids (26-270 a.a.) and having a molecular mass of 29kDa. The KDSR is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The KDSR solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol, 0.1M NaCl and 0.1mM PMSF.
Purity
KDSR purity was found to be greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
3-ketodihydrosphingosine reductase (KDSR) is a 332 amino acid multi-pass membrane protein which localizes to the ER and is a member of the short-chain dehydrogenases/reductases (SDR) family. KDSR is a secreted protein that is weakly expressed in hematopoietic tissue. Furthermore, KDSR catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS). The putative active site residues of KDSR are found on the cytosolic side of the endoplasmic reticulum membrane. Chromosomal rearrangement in the KDSR gene is a cause of follicular lymphoma, aka type II chronic lymphatic leukemia.
-
Synonyms
3-ketodihydrosphingosine reductase, KDS reductase, 3-dehydrosphinganine reductase, Follicular variant translocation protein 1, FVT-1, KDSR, FVT1, DHSR, SDR35C1, FLJ36555, FLJ92680.
-
Physical Appearance
The KDSR is supplied as a 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 MKPLALPGAH VVVTGGSSGI GKCIAIECYK QGAFITLVAR NEDKLLQAKK EIEMHSINDK QVVLCISVDV SQDYNQVENV IKQAQEKLGP VDMLVNCAGM AVSGKFEDLE VSTFERLMSI NYLGSVYPSR AVITTMKERR VGRIVFVSSQ AGQLGLFGFT AYSASKFAIR GLAEALQMEV KPYNVYITVA YPPDTDTPGF AEENRTKPLE TRLISETTSV CKPEQVAKQI VKDAIQGNFN SSLGSD.
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 :
TRXR E.ColiDescription:
Thioredoxin Reductase E.Coli Recombinant
TRXB, TRXR, Thioredoxin Reductase.
Product # :
ENZ-507Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
TRXR E.coli Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 321 amino acids (1-321 a.a.) and having a molecular mass of 34.6 kDa. TRXR protein is purified by standard chromatography.
Source
Escherichia Coli.
Formulation
TRXR E.Coli solution containing 20mM Tris HCl pH-8, 1mM DTT, and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is 4-5 units/ml, and was measured in a coupled assay with DTNB and NADPH. The amount of TNB generated by NADPH was measured in absorbance at 412 nm.More Info
-
Introduction
TRXR is a ubiquitous enzyme which participates in various cellular processes such as cell growth, p53 activity, and protection against oxidation stress. The mammalian Thioredoxin reductase cleaves thioredoxins as well as non-disulfide substrates such as selenite, lipoic acids, lipid hydroperoxides, and hydrogen peroxidec.
-
Synonyms
TRXB, TRXR, Thioredoxin Reductase.
-
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
MGTTKHSKLL ILGSGPAGYT AAVYAARANL QPVLITGMEK GGQLTTTTEV ENWPGDPNDL TGPLLMERMH EHATKFETEI IFDHINKVDL QNRPFRLNGD NGEYTCDALI IATGASARYL GLPSEEAFKG RGVSACATCD GFFYRNQKVA VIGGGNTAVE EALYLSNIAS EVHLIHRRDG FRAEKILIKR LMDKVENGNI ILHTNRTLEE VTGDQMGVTG VRLRDTQNSD NIESLDVAGL FVAIGHSPNT AIFEGQLELE NGYIKVQSGI HGNATQTSIP GVFAAGDVMD HIYRQAITSA GTGCMAALDA ERYLDGLADA K.
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 :
CKBB Human, ActiveDescription:
Creatine Kinase Brain Human Recombinant, Active
Creatine kinase B-type, EC 2.7.3.2, Creatine kinase B chain, B-CK, CKB, CKBB, CKBBI.
Product # :
CKI-268Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CKBB Human Recombinant produced in Pichia Pastoris is a dimeric glycosylated full length polypeptide chain comprised of 2 identical B subunits and having an identical amino acid sequence compared to the native enzyme, purified under non-denaturing conditions and having a Mw of 47kDa The CKBB is purified by proprietary chromatographic techniques.
Source
Pichia Pastoris.
Formulation
CKBB Human contains 10Mm Bis-Tris-HCl pH-6.0, 50% glycerol, 0.5mM EDTA and 0.5mM DTT.
Purity
Greater than 95.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The biological activity of CKBB was measured by the enzymatic activity of Creatine phosphokinase procedure No.45-UV, 1IU-1 µmole creatine phosphate was 854 IU/mg at 37 degrees celsius corresponding to a Specific Activity of 1,171ng/ml.More Info
-
Introduction
Creatine Kinase BB is a cytoplasmic enzyme involved in energy homeostasis. The encoded protein reversibly catalyzes the transfer of phosphate between ATP and various phosphogens such as creatine phosphate. It acts as a homodimer in brain as well as in other tissues, and as a heterodimer with a similar muscle isozyme in heart. The encoded protein is a member of the ATP:guanido phosphotransferase protein family. A pseudogene of this gene has been characterized.
-
Synonyms
Creatine kinase B-type, EC 2.7.3.2, Creatine kinase B chain, B-CK, CKB, CKBB, CKBBI.
-
Physical Appearance
Sterile Filtered colourless liquid formulation.
-
Stability
CKBB should be stored below -18°C. Please prevent freeze-thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ARG2 HumanDescription:
Arginase Type II Human Recombinant
Kidney Arginase, Non-Hepatic Arginase, EC 3.5.3.1, Arginase-2, Type II arginase, Kidney-type arginase, Arginase-2 mitochondrial.
Product # :
ENZ-526Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
ARG2 Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (23-354 a.a.) and having a molecular mass of 38.3 kDa. The ARG2 is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ARG2 Human solution containing 20mM Tris-HCl pH-8, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
ARG2 participates in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to NO synthase. Since NO synthase is found in the penile corpus cavernosum smooth muscle, the clitoral corpus cavernosum and the vagina, ARG2 takes part in both male and female sexual arousal and therefore a potential target for the treatment of male and female sexual arousal disorders.
-
Synonyms
Kidney Arginase, Non-Hepatic Arginase, EC 3.5.3.1, Arginase-2, Type II arginase, Kidney-type arginase, Arginase-2 mitochondrial.
-
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 MVHSVAVIGA PFSQGQKRKG VEHGPAAIRE AGLMKRLSSL GCHLKDFGDL SFTPVPKDDL YNNLIVNPRS VGLANQELAE VVSRAVSDGY SCVTLGGDHS LAIGTISGHA RHCPDLCVVW VDAHADINTP LTTSSGNLHG QPVSFLLREL QDKVPQLPGF SWIKPCISSA SIVYIGLRDV DPPEHFILKN YDIQYFSMRD IDRLGIQKVM ERTFDLLIGK RQRPIHLSFD IDAFDPTLAP ATFTPVVGGL TYREGMYIAE EIHNTGLLSA LDLVEVNPQL ATSEEEAKTT ANLAVDVIAS SFGQTREGGH IVYDQLPTPS SPDESENQAR VRI.
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 :
GPT Human, His ActiveDescription:
Glutamic-Pyruvate Transaminase, His Tag Active Human Recombinant
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
Product # :
ENZ-1000Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
GPT Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 516 amino acids (1-496) and having a molecular mass of 56.8 kDa.GPT is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GPT solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 100units/mg, and is defined as the amount of enzyme that cleaves 1umole of L-Alanine to L-Glutamate per minute at pH 7.5 at 37C.
More Info
-
Introduction
GPT catalyzes the reversible transamination between alanine and 2-oxoglutarate to create pyruvate and glutamate. GPT has a crucial part in the intermediary metabolism of glucose and amino acids. GPT is broadly used as an indicator of liver reliability or hepatocellular destruction in clinical tests.
-
Synonyms
Glutamic-pyruvate transaminase (alanine aminotransferase), GPT1, ALT1, AAT1, Glutamic-alanine transaminase 1, EC 2.6.1.2.
-
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 MASSTGDRSQ AVRHGLRAKV LTLDGMNPRV RRVEYAVRGP IVQRALELEQ ELRQGVKKPF TEVIRANIGD AQAMGQRPIT FLRQVLALCV NPDLLSSPNF PDDAKKRAER ILQACGGHSL GAYSVSSGIQ LIREDVARYI ERRDGGIPAD PNNVFLSTGA SDAIVTVLKL LVAGEGHTRT GVLIPIPQYP LYSATLAELG AVQVDYYLDE ERAWALDVAE LHRALGQARD HCRPRALCVI NPGNPTGQVQ TRECIEAVIR FAFEERLFLL ADEVYQDNVY AAGSQFHSFK KVLMEMGPPY AGQQELASFH STSKGYMGEC GFRGGYVEVV NMDAAVQQQM LKLMSVRLCP PVPGQALLDL VVSPPAPTDP SFAQFQAEKQ AVLAELAAKA KLTEQVFNEA PGISCNPVQG AMYSFPRVQL PPRAVERAQE LGLAPDMFFC LRLLEETGIC VVPGSGFGQR EGTYHFRMTI LPPLEKLRLL LEKLSRFHAK FTLEYS
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 :
CKBB Human HisDescription:
Creatine Kinase Brain Human Recombinant, His Tag
EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.
Product # :
CKI-274Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CKBB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 401 amino acids (1-381 a.a.) and having a molecular mass of 44.8 kDa. The CKB is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CKBB Human solution containing 20mM Trsi pH-8, 1mM DTT, & 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CKB is a cytoplasmic enzyme that takes part in energy homeostasis. CKB enzyme reversibly catalyzes the transfer of phosphate among ATP and various phosphogens such as creatine phosphate. CKB functions as a homodimer in the brain as well as in different tissues, and as a heterodimer with a similar muscle isozyme in heart. Creatine kinases supply the energy of phosphate hydrolysis essential to drive the normal role of many cellular systems including muscle, tumor and cancer cells.
-
Synonyms
EC 2.7.3.2, Creatine kinase B chain, Creatine kinase B type, CKB, CKBBB, B-CK, Creatine Kinase Brain.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
CKBB Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPFSNSHNAL KLRFPAEDEF PDLSAHNNHM AKVLTPELYA ELRAKSTPSG FTLDDVIQTG VDNPGHPYIM TVGCVAGDEE SYEVFKDLFD PIIEDRHGGY KPSDEHKTDL NPDNLQGGDD LDPNYVLSSR VRTGRSIRGF CLPPHCSRGE RRAIEKLAVE ALSSLDGDLA GRYYALKSMT EAEQQQLIDD HFLFDKPVSP LLLASGMARD WPDARGIWHN DNKTFLVWVN EEDHLRVISM QKGGNMKEVF TRFCTGLTQI ETLFKSKDYE FMWNPHLGYI LTCPSNLGTG LRAGVHIKLP NLGKHEKFSE VLKRLRLQKR GTGGVDTAAV GGVFDVSNAD
RLGFSEVELV QMVVDGVKLL IEMEQRLEQG QAIDDLMPAQ K.
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 :
BPGM HumanDescription:
2,3-Bisphosphoglycerate Mutase Human Recombinant
Bisphosphoglycerate mutase, EC 5.4.2.4, BPGM, 2,3-bisphosphoglycerate mutase erythrocyte, 2,3-bisphosphoglycerate synthase, BPG-dependent PGAM.
Product # :
ENZ-505Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
BPGM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 267 amino acids (1-259 a.a.) and having a molecular mass of 31 kDa. The BPGM is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BPGM solution (0.5mg/ml) contains 20mM Tris-HCl (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
BPGM is found at high concentrations in red blood cells where it binds to and decreases the oxygen affinity of hemoglobin. PGM deficiency increases the oxygen affinity of cells. BPGM is a multifunctional enzyme that catalyzes 2,3-DPG synthesis through its synthetase activity, and 2,3-DPG degradation using its phosphatase activity. BPGM has phosphoglycerate phosphomutase activity. Mutations in BPGM cause hemolytic anemia. BPGM catalyzes the reaction of EC 5.4.2.1 (mutase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.
-
Synonyms
Bisphosphoglycerate mutase, EC 5.4.2.4, BPGM, 2,3-bisphosphoglycerate mutase erythrocyte, 2,3-bisphosphoglycerate synthase, BPG-dependent PGAM.
-
Physical Appearance
Sterile Filtered clear 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
MSKYKLIMLR HGEGAWNKEN RFCSWVDQKL NSEGMEEARN CGKQLKALNF EFDLVFTSVL NRSIHTAWLI LEELGQEWVP VESSWRLNERHYGALIGLNR EQMALNHGEE QVRLWRRSYN VTPPPIEESH PYYQEIYNDR RYKVCDVPLD QLPRSESLKD VLERLLPYWN ERIAPEVLRG KTILISAHGN SSRALLKHLE GISDEDIINI TLPTGVPILL ELDENLRAVG PHQFLGDQEA IQAAIKKVED QGKVKQAKKL 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 :
CDA HumanDescription:
Cytidine Deaminase Human Recombinant
Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.
Product # :
ENZ-007Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
CDA 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 166 amino acids (1-146 a.a.) and having a molecular mass of 18.3kDa. The CDA is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDA solution (0.5mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0), 1mM DTT, 2mM EDTA, 100mM NaCl and 40% Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 10,000pmol/min/ug, and is defined as the amount of required to deaminate 1.0pmole of cytidine per min at pH 7.5 at 25C.
More Info
-
Introduction
Cytidine deaminase (CDA) is an enzyme that scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. CDA is one of several deaminases responsible for maintaining the cellular pyrimidine pool. CDA also catalyzes the deamination of chemotherapeutic cytosine nucleoside analogs such as Ara-C and 5-azacytidine, which results in the loss of their cytotoxic and antitumor function. CDA can form homotetramers and is generally expressed in granulocytes. Mutations in the CDA gene are linked to decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias.
-
Synonyms
Cytidine deaminase, Cytidine aminohydrolase, CDA, CDD.
-
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 MAQKRPACTL KPECVQQLLV CSQEAKQSAY CPYSHFPVGA ALLTQEGRIF KGCNIENACY PLGICAERTA IQKAVSEGYK DFRAIAIASD MQDDFISPCG ACRQVMREFG TNWPVYMTKP DGTYIVMTVQ ELLPSSFGPE DLQKTQ.
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 :
GYG1 HumanDescription:
Glycogenin-1 Human Recombinant
Glycogenin-1, GYG1, GYG.
Product # :
ENZ-431Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GYG1 Human Recombinant fused with a 32 amino acid His-T7 tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 365 amino acids (1-333 a.a.) and having a molecular mass of 41.2kDa.The GYG1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GYG1 solution contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Glycogenin-1 (GYG1) is an enzyme involved in glycogen biosynthesis. GYG1 is the chief enzyme involved in glycogen polymerisation. Glycogenin-1 is vital for the function of self-glucosylates, using an inter-subunit mechanism, to form an oligosaccharide primer which acts as substrate for glycogen synthase. In addition, GYG1 has a role in regulating glycogen metabolism and the achievement of maximal glycogen levels in skeletal muscle. GYG1 mRNA and protein content and activity increase in the muscle during recovery from prolonged and exhaustive exercise. GYG1 is inactivated with glycogen catabolism which concurs with an increase in glycogenin gene expression as exercise and glycogenolysis advance. Glycogenin will remain covalently attached to the reducing end of the glycogen molecule.
-
Synonyms
Glycogenin-1, GYG1, GYG.
-
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
MHHHHHHMAS MTGGQQMGRD LYDDDDKDRW GSMTDQAFVT LTTNDAYAKG ALVLGSSLKQ HRTTRRLVVL ATPQVSDSMR KVLETVFDEV IMVDVLDSGD SAHLTLMKRP ELGVTLTKLH CWSLTQYSKC VFMDADTLVL ANIDDLFDRE ELSAAPDPGW PDCFNSGVFV YQPSVETYNQ LLHLASEQGS FDGGDQGILN TFFSSWATTD IRKHLPFIYN LSSISIYSYL PAFKVFGASA KVVHFLGRVK PWNYTYDPKT KSVKSEAHDP NMTHPEFLIL WWNIFTTNVL PLLQQFGLVK DTCSYVNVED VSGAISHLSL GEIPAMAQPF VSSEERKERW EQGQADYMGA DSFDNIKRKL DTYLQ.
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 :
NAT6 HumanDescription:
N-Acetyltransferase 6 Human Recombinant
Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-2.
Product # :
ENZ-410Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human NAT6 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 328 amino acids (1-308 a.a.) and having a molecular mass of 35.9 kDa. NAT6 is fused to a 20 amino acid His Tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The NAT6 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
NAT6 is an enzyme that catalyzes the transfer of acetyl groups from acetyl-CoA to acrylamines. NAT6 is located mainly in the cytoplasm and its activity has been recognized by its feasibility to acetylate the N-terminus of proteins using a ping-pong-like mechanism and by its substrate specificity. Given that the NAT6 gene maps to the chromosomal region 3p21.3, which includes at least one tumor suppressor gene, the function of NAT6 plays an important role in cancer.
-
Synonyms
Protein fusion-2, FUS2, FUS-2, NAT6, N-acetyltransferase 6, Protein fus-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 MQELTLSPGP AKLTPTLDPT HRMELILSTS PAELTLDPAC QPKLPLDSTC QPEMTFNPGP TELTLDPEHQ PEETPAPSLA ELTLEPVHRR PELLDACADL INDQWPRSRT SRLHSLGQSS DAFPLCLMLL SPHPTLEAAP VVVGHARLSR VLNQPQSLLV ETVVVARALR GRGFGRRLME GLEVFARARG FRKLHLTTHD QVHFYTHLGY QLGEPVQGLV FTSRRLPATL LNAFPTAPSP RPPRKAPNLT AQAAPRGPKG PPLPPPPPLP ECLTISPPVP SGPPSKSLLE TQYQNVRGRP IFWMEKDI.
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 :
UBE2B HumanDescription:
Ubiquitin Conjugating Enzyme E2B Human Recombinant
Ubiquitin-conjugating enzyme E2 B, EC 6.3.2.19, Ubiquitin-protein ligase B, Ubiquitin carrier protein B, HR6B, hHR6B, E2-17 kDa UBC2, HHR6B, RAD6B, E2-17kDa, UBE2B.
Product # :
ENZ-340Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Ubiquitin Conjugating Enzyme E2B Human Recombinant produced in E.coli is a 19 kDa protein containing 166 amino acids.The UE2B protein contains 6xHis tag and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2μm filtered concentrated (1 mg/ml) solution in 1X PBS and 1mM DTT, pH 7.5.
Purity
Greater than 95.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
More Info
-
Introduction
This E2 enzyme encodes for the human homolog of the yeast DNA repair gene RAD6, which is induced by DNA damaging agents. UBE2B can conjugate ubiquitin to histone H2A in an E3- independent manner in vitro, and is essential for the multi-ubiquitination and degradation of N-end rule substrates. Additionally, UBE2B may have a role in sepsis-induced muscle protein proteolysis and cancer-induced cachexia.
-
Synonyms
Ubiquitin-conjugating enzyme E2 B, EC 6.3.2.19, Ubiquitin-protein ligase B, Ubiquitin carrier protein B, HR6B, hHR6B, E2-17 kDa UBC2, HHR6B, RAD6B, E2-17kDa, UBE2B.
-
Physical Appearance
Sterile Filtered white lyophilized powder.
-
Stability
Lyophilized UBE2B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution UBE2B 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 UBE2B in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
MHHHHHHAMGQLRSMSTPARRRLMRDFKRLQEDPPVGVSGAPSENN
IMQWNAVIFGPEGTPFEDGTFKLVIEFSEEYPNKPPTVRFLSKMFHPNVY
ADGSICLDILQNRWSPTYDVSSILTSIQSLLDEPNPNSPANSQAAQLYQE
NKREYEKRVSAIVEQSWNDS.
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 :
MTHFS HumanDescription:
5,10-Methenyltetrahydrofolate Synthetase Human Recombinant
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
Product # :
ENZ-096Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
MTHFS produced in E.Coli is a single, non-glycosylated polypeptide chain containing 223 amino acids (1-203a.a.) and having a molecular mass of 25.4 kDa. MTHFS is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MTHFS protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 5mM DTT and 30% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
MTHFS is a cytosolic protein which takes part in the formate metabolic process. MTHFS along with a magnesium cofactor catalyzes the ATP-dependent reaction which reduces 5-formyltetrahydrofolate (5-MTHF) to 5,10-methenyltetrahydrofolate(MTHF). MTHF is the substrate used by MTHFR (methylenetetrahydrofolate reductase) to generate 5-MTHF. In addition, MTHF is a coenzyme used in thymidine biosynthesis by thymidylate synthase (FAD).
-
Synonyms
5,10-methenyltetrahydrofolate synthetase (5-formyltetrahydrofolate cyclo-ligase), HsT19268, Methenyl-THF synthetase, FLJ30410, EC 6.3.3.2.
-
Physical Appearance
Sterile Filtered clear solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAAAVSSAK RSLRGELKQR LRAMSAEERL RQSRVLSQKV IAHSEYQKSK RISIFLSMQD EIETEEIIKD IFQRGKICFI PRYRFQSNHM DMVRIESPEE ISLLPKTSWN IPQPGEGDVR EEALSTGGLD LIFMPGLGFD KHGNRLGRGK GYYDAYLKRC LQHQEVKPYT LALAFKEQIC LQVPVNENDM KVDEVLYEDS STA
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 :
GOT2 HumanDescription:
Glutamic-Oxaloacetic Transaminase 2 Human Recombinant
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
Product # :
ENZ-684Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GOT2 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 424 amino acids (30-430 a.a.) and having a molecular mass of 47kDa. The GOT2 fused to a 23 amino acid his tag at N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GOT2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GOT2 is a pyridoxal phosphate-dependent enzyme which is found in cytoplasmic and inner-membrane mitochondrial forms, GOT1 and GOT2. GOT2 is invloved in amino acid metabolism and the urea and tricarboxylic acid cycles. The 2 enzymes are homodimeric and demonstrate close homology.
-
Synonyms
EC 2.6.1.1, Aspartate aminotransferase 1, Transaminase A, GIG18.
-
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 MGSSSWWTHV EMGPPDPILG VTEAFKRDTN SKKMNLGVGA YRDDNGKPYV LPSVRKAEAQ IAAKNLDKEY LPIGGLAEFC KASAELALGE NSEVLKSGRF VTVQTISGTG ALRIGASFLQ RFFKFSRDVF LPKPTWGNHT PIFRDAGMQL QGYRYYDPKT CGFDFTGAVE DISKIPEQSV LLLHACAHNP TGVDPRPEQW KEIATVVKKR NLFAFFDMAY QGFASGDGDK DAWAVRHFIE QGINVCLCQS YAKNMGLYGE RVGAFTMVCK DADEAKRVES QLKILIRPMY SNPPLNGARI AAAILNTPDL RKQWLQEVKV MADRIIGMRT QLVSNLKKEG STHNWQHITD QIGMFCFTGL KPEQVERLIK EFSIYMTKDG RISVAGVTSS NVGYLAHAIH QVTK.
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 :
Latexin HumanDescription:
Latexin Human Recombinant
LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.
Product # :
ENZ-407Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human Latexin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids and having a molecular mass of 25.7kDa. Latexin is purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The Latexin protein solution contains 20mM Tris-HCl, pH-7.5, 50mM NaCl and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Latexin enzyme is a carboxypeptidase A inhibitor that is highly expressed in the heart, prostate, ovary, kidney, pancrease, brain and colon. Latexin has no noticeable sequence resemblance with plant and parasite inhibitors, however it is related to a human putative tumor suppressor protein, TIG1. Latexin is down-regulated in the presenilin-1-deficient mouse brain, thus putatively playing a role in Alzheimer's disease.
-
Synonyms
LXN, TCI, ECI, Latexin, Endogenous carboxypeptidase inhibitor, Tissue carboxypeptidase inhibitor, MUM.
-
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
MEIPPTNYPA SRAALVAQNY INYQQGTPHR VFEVQKVKQA SMEDIPGRGH KYRLKFAVEE IIQKQVKVNC TAEVLYPSTG QETAPEVNFTFEGETGKNPD EEDNTFYQRL KSMKEPLEAQ NIPDNFGNVS PEMTLVLHLA WVACGYIIWQ NSTEDTWYKM VKIQTVKQVQ RNDDFIELDYTILLHNIASQ EIIPWQMQVL WHPQYGTKVK HNSRLPKEVQ LE.
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 :
CBR3 AntibodyDescription:
Carbonyl Reductase-3, Mouse Anti Human
Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.
Product # :
ANT-393Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- formulation
- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
-
Introduction
CBR3 catalyzes the reduction of a large number of biologically and pharmacologically active carbonyl compounds to their corresponding alcohols. CBR3 is one of several monomeric NADPH-dependent oxidoreductases. Furthermore, CBR3 contains 3 exons spanning 11.2 kilobases and is strongly linked to another carbonyl reductase gene, the CBR1. It was suggested that CBR3 mediates 9-cis-retinoic acid-induced cytostatis and is a potential prognostic marker for oral malignancy. CBR3 is identified in the ovary, pancreas, intestine, colon, kidney, brain, thymus, lung, heart, liver, spleen, leukocyte, prostate and the testis. Polymorphisms in CBR3 may give an explanation to interindividual and interethnic variability of doxorubicin pharmacokinetics and pharmacodynamics.
-
Synonyms
Carbonyl reductase [NADPH] 3, NADPH-dependent carbonyl reductase 3, CBR3, carbonyl reductase 3, hCBR3, SDR21C2.
-
Immunogen
Anti-human CBR3 mAb is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human CBR3 amino acids 1-277 purified from E. coli.
-
Ig Subclass
Mouse IgG2b heavy chain and ? light chain.
-
Clone
PAT7E8AT.
-
Applications
CBR3 antibody has been tested by ELISA, Western blot analysis, Flow cytometry and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
-
Type
Mouse Anti Human Monoclonal.
-
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
-
Purification Method
CBR3 antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.
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 :
MIOX HumanDescription:
Myo-Inositol Oxygenase Human Recombinant
Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.
Product # :
ENZ-812Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
MIOX Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Met1-Trp285) containing 295 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 34.2kDa.
Source
Escherichia Coli.
Formulation
MIOX was filtered (0.4 µm) and lyophilized in 20mM Tris buffer, 50mM NaCl and 5% (w/v) trehalose, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Inositol oxygenase is a non-heme di-iron enzyme which oxidizes myo-inositol to glucuronic acid. In addition, inositol oxygenase oxidizes the less abundant chiro isomer of inositol. MIOX enzyme is a component of the only known pathway for the catabolism of inositol in humans. MIOX is expressed mostly in the kidneys. Reduction of Inositol Oxygenase and accumulation of polyols, such as inositol and xylitol, have been implicated as contributing factors in complications linked with diabetes.
-
Synonyms
Myo-Inositol Oxygenase, Kidney-Specific Protein 32, Aldehyde Reductase (Aldose Reductase) Like 6, Renal-Specific Oxidoreductase, Aldehyde Reductase-Like 6, MI Oxygenase, EC 1.13.99.1, ALDRL6, Inositol Oxygenase, KSP32, RSOR, MIOX.
-
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.
-
Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. MIOX is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
-
Amino Acid Sequence
MKHHHHHHASMKVTVGPDPS LVYRPDVDPE VAKDKASFRN YTSGPLLDRV FTTYKLMHTH QTVDFVRSKH AQFGGFSYKK MTVMEAVDLL DGLVDESDPD VDFPNSFHAF QTAEGIRKAH PDKDWFHLVG LLHDLGKVLA LFGEPQWAVV GDTFPVGCRP QASVVFCDST FQDNPDLQDP RYSTELGMYQ PHCGLDRVLM SWGHDEYMYQ VMKFNKFSLP PEAFYMIRFH SFYPWHTGRD YQQLCSQQDL AMLPWVREFN KFDLYTKCPD LPDVDKLRPY YQGLIDKYCP GILSW.
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 :
HEXA HumanDescription:
Hexosaminidase A Human Recombinant
TSD, hexosaminidase A, Beta-hexosaminidase subunit alpha, Beta-N-acetylhexosaminidase subunit alpha, Hexosaminidase subunit A, N-acetyl-beta-glucosaminidase subunit alpha.
Product # :
ENZ-683Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
HEXA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 464 amino acids (89-529 a.a) and having a molecular mass of 52.9 kDa.HEXA is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
HEXA 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.
More Info
-
Introduction
HEXA is the alpha subunit of the lysosomal enzyme beta-hexosaminidase which, combined with the cofactor GM2 activator protein, catalyzes the degradation of the ganglioside GM2, and other molecules having N-acetyl hexosamines terminus. The two subunits composing Beta-hexosaminidase, alpha and beta, belong to the glycosyl hydrolases family and are encoded by distinct genes. Alpha subunit gene mutations can cause Tay-Sachs disease (GM2-gangliosidosis type I).
-
Synonyms
TSD, hexosaminidase A, Beta-hexosaminidase subunit alpha, Beta-N-acetylhexosaminidase subunit alpha, Hexosaminidase subunit A, N-acetyl-beta-glucosaminidase subunit alpha.
-
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 MGSTLEKNVL VVSVVTPGCN QLPTLESVEN YTLTINDDQC LLLSETVWGA LRGLETFSQL VWKSAEGTFF INKTEIEDFP RFPHRGLLLD TSRHYLPLSS ILDTLDVMAY NKLNVFHWHL VDDPSFPYES FTFPELMRKG SYNPVTHIYT AQDVKEVIEY ARLRGIRVLA EFDTPGHTLS WGPGIPGLLT PCYSGSEPSG TFGPVNPSLN NTYEFMSTFF LEVSSVFPDF YLHLGGDEVD FTCWKSNPEI QDFMRKKGFG EDFKQLESFY IQTLLDIVSS YGKGYVVWQE VFDNKVKIQP DTIIQVWRED IPVNYMKELE LVTKAGFRAL LSAPWYLNRI SYGPDWKDFY VVEPLAFEGT PEQKALVIGG EACMWGEYVD NTNLVPRLWP RAGAVAERLW SNKLTSDLTF AYERLSHFRC ELLRRGVQAQ PLNVGFCEQE FEQT.
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 :
IDI2 HumanDescription:
Isopentenyl-Diphosphate Delta Isomerase 2 Human Recombinant
Isopentenyl-diphosphate Delta-isomerase 2, Isopentenyl pyrophosphate isomerase 2, IPP isomerase 2, IPPI2, IDI2.
Product # :
ENZ-107Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
IDI2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 247 amino acids (1-227 a.a.) and having a molecular mass of 28.9kDa.IDI2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
IDI2 solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 0.1mM PMSF.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
Isopentenyl-diphosphate Delta-isomerase 2 (IDI2) is a member of the IPP isomerase type 1 family. IDI2 catalyzes the 1,3-allylic reorganization of the homoallylic substrate isopentenyl (IPP) to its extremely electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
-
Synonyms
Isopentenyl-diphosphate Delta-isomerase 2, Isopentenyl pyrophosphate isomerase 2, IPP isomerase 2, IPPI2, IDI2.
-
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 MSDINLDWVD RRQLQRLEEM LIVVDENDKV IGADTKRNCH LNENIEKGLL HRAFSVVLFN TKNRILIQQR SDTKVTFPGY FTDSCSSHPL YNPAELEEKD AIGVRRAAQR RLQAELGIPG EQISPEDIVF MTIYHHKAKS DRIWGEHEIC YLLLVRKNVT LNPDPSETKS ILYLSQEELW ELLEREARGE VKVTPWLRTI AERFLYRWWP HLDDVTPFVE LHKIHRV.
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 :
GGH HumanDescription:
Gamma-Glutamyl Hydrolase Human Recombinant
Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.
Product # :
ENZ-242Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GGH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 315 amino acids (25-318) and having a molecular mass of 35.9kDa.GGH is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GGH solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
GGH is a homodimeric protein which catalyzes the cleavage of the gamma-glutamyl chain of folylpoly-gamma-glutamyl substrates. GGH is a vital enzyme in folyl and antifolyl poly-gamma-glutamate metabolism and it has a significant part in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of antifolates and pteroylpolyglutamates.
-
Synonyms
Gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase), Gamma-Glu-X carboxypeptidase, gamma-glutamyl hydrolase, Conjugase, GH, EC 3.4.19.9.
-
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 MRPHGDTAKK PIIGILMQKC RNKVMKNYGR YYIAASYVKY LESAGARVVP VRLDLTEKDY EILFKSINGI LFPGGSVDLR RSDYAKVAKI FYNLSIQSFD DGDYFPVWGT CLGFEELSLL ISGECLLTAT DTVDVAMPLN FTGGQLHSRM FQNFPTELLL SLAVEPLTAN FHKWSLSVKN FTMNEKLKKF FNVLTTNTDG KIEFISTMEG YKYPVYGVQW HPEKAPYEWK NLDGISHAPN AVKTAFYLAE FFVNEARKNN HHFKSESEEE KALIYQFSPI YTGNISSFQQ CYIFD
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 :
CTSE MouseDescription:
Cathepsin-E Mouse Recombinant
CTSE, A430072003Rik, C920004C08Rik, CatE, CE.
Product # :
ENZ-1140Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CTSE Mouse produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 385 amino acids ( 21-397 a.a.) and having a molecular mass of 41.8 kDa.CTSE is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
CTSE protein solution ( 0.5mg/ml ) contains PBS (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
CTSE or cathepsin E is an intracellular aspartic protease from the pepsin protein family. CTSE has a crucial part in protein degradation, creating bioactive proteins & processing antigens. The enzyme is responsible for cleaving at B site, Swedish mutant of amyloid precursor protein and the enzyme shows reactivity with the wild-type APP.
-
Synonyms
CTSE, A430072003Rik, C920004C08Rik, CatE, CE.
-
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
ALHRVPLRRH QSLRKKLRAQ GQLSEFWRSH NLDMTRLSES CNVYSSVNEP LINYLDMEYF GTISIGTPPQ NFTVIFDTGS SNLWVPSVYC TSPACKAHPV FHPSQSDTYT EVGNHFSIQY GTGSLTGIIG ADQVSVEGLT VDGQQFGESV KEPGQTFVNA EFDGILGLGY PSLAAGGVTP VFDNMMAQNL VALPMFSVYL SSDPQGGSGS ELTFGGYDPS HFSGSLNWIP VTKQAYWQIA
LDGIQVGDTV MFCSEGCQAI VDTGTSLITG PPDKIKQLQE AIGATPIDGE YAVDCATLDT MPNVTFLINE VSYTLNPTDY ILPDLVEGMQ FCGSGFQGLD IPPPAGPLWI LGDVFIRQFY SVFDRGNNQV GLAPAVPLEH 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.