Search results
1000 results found for “SPSB”
Name
Description
Product #
Price
Quantity
Shipping Method
- 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 :
GroEL E.ColiDescription:
GroEL (HSP60) E.Coli Recombinant
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.
Product # :
HSP-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant GroEL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 548 amino acids (1-548) and having a molecular mass of 57.3kDa. GroEL is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The groEL protein contains 25mM Tris buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
GroEL protein is the major heat shock protein of E.coli and belongs to the chaperonin (HSP60) family. GroEL protein prevents misfolding of proteins and promotes the refolding and proper assembly of unfolded polypeptiedes generated under stress condition.
-
Synonyms
CPN60, GROEL, HSP60, HSP65, SPG13, CHA60, GROL, crpA, mopA, 60 kDa chaperonin, Protein Cpn60, groEL protein, b4143, JW4103.
-
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
MAAKDVKFGN DARVKMLRGV NVLADAVKVT LGPKGRNVVL DKSFGAPTIT KDGVSVAREIELEDKFENMG AQMVKEVASK ANDAAGDGTT TATVLAQAII TEGLKAVAAG MNPMDLKRGIDKAVTAAVEE LKALSVPCSD SKAIAQVGTI SANSDETVGK LIAEAMDKVG KEGVITVEDGTGLQDELDVV EGMQFDRGYL SPYFINKPET GAVELESPFI LLADKKISNI REMLPVLEAVAKAGKPLLII AEDVEGEALA TAVVNTIRGI VKVAAVKAPG FGDRRKAMLQ DIATLTGGTVISEEIGMELE KATLEDLGQA KRVVINKDTT TIIDGVGEEA AIQGRVAQIR QQIEEATSDYDREKLQERVA KLAGGVAVIK VGAATEVEMK EKKARVEDAL HATRAAVEEG VVAGGGVALIRVASKLADLR GQNEDQNVGI KVALRAMEAP LRQIVLNCGE EPSVVANTVK GGDGNYGYNAATEEYGNMID MGILDPTKVT RSALQYAASV AGLMITTECM VTDLPKNDAA DLGAAGGMGG MGGMGGMM.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GroES E.ColiDescription:
GroES (HSP10) E.Coli Recombinant
CPN10, GROES, HSP10, HSPE1, 10 kDa chaperonin, Protein Cpn10, groES protein, 11.2 kDa stress response protein, Heat shock protein 10.
Product # :
HSP-005Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant GroES produced in E.Coli is a single, non-glycosylated polypeptide chain containing 97 amino acids and having a molecular mass of 10.4 kDa.
Source
Escherichia Coli.
Formulation
The GroES protein (1mg/ml) contains 25mM Tris-HCl buffer (pH 7.5), 100mM NaCl, 5mM DTT and 10% Glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
-
Introduction
GroES protein is the co-chaperonin of GroES in E.coli and assists protein folding. GroEL mediated folding requires the co-chaperonin GroES which is essential for viability. GroES is composed of a single heptameric ring of 10kDa subunits that binds to the ends of the GroEL cylinder. GroES gene was amplified by PCR from E.coli and cloned into an expression vector. This protein was overexpressed in E.coli and was purified by using conventional chromatography techniques.
-
Synonyms
CPN10, GROES, HSP10, HSPE1, 10 kDa chaperonin, Protein Cpn10, groES protein, 11.2 kDa stress response protein, Heat shock protein 10.
-
Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MNIRPLHDRV IVKRKEVETK SAGGIVLTGS AAAKSTRGEV LAVGNGRILE GEVKPLDVKVGDIVIFNDG YGVKSEKIDN EEVLIMSESD ILAIVEA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GSTA4 HumanDescription:
Glutathione S-Transferase Alpha 4 Human Recombinant
Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.
Product # :
ENZ-600Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GSTA4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 246 amino acids (1-222) and having a molecular mass of 28.3kDa.GSTA4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The GSTA4 solution (1mg/ml) contains 20mM Tris-HCl buffer, pH8.0, 20% glycerol, 2mM DTT and 100mM NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Glutathione S-transferase A4 (GSTA4) is a member of the GST superfamily. The GSTA4 enzyme is involved in cellular defense against toxic, carcinogenic, and pharmacologically active electrophilic compounds. GSTA4 shows an especially high activity with reactive carbonyl compounds such as alk-2-enals. GSTA4 is extremely effective in catalyzing the conjugate addition of reduced glutathione to 4-hydroxynonenal, which is an important product of peroxidative degradation of arachidonic acid and a frequently used biomarker for oxidative damage in tissue. The GSTA4 enzyme is expressed at a high level in the brain, placenta, and skeletal muscle and much lower in the lung and liver.
-
Synonyms
Glutathione S-transferase A4, GST class-alpha member 4, Glutathione S-transferase A4-4, GSTA4, GSTA4-4.
-
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 MGSHMAARPK LHYPNGRGRM ESVRWVLAAA GVEFDEEFLE TKEQLYKLQD GNHLLFQQVP MVEIDGMKLV QTRSILHYIA DKHNLFGKNL KERTLIDMYV EGTLDLLELL IMHPFLKPDD QQKEVVNMAQ KAIIRYFPVF EKILRGHGQS FLVGNQLSLA
DVILLQTILA LEEKIPNILS AFPFLQEYTV KLSNIPTIKR FLEPGSKKKP PPDEIYVRTV YNIFRP.
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 :
CMBL HumanDescription:
Carboxymethylenebutenolidase Human Recombinant
Carboxymethylenebutenolidase homolog, CMBL, JS-1.
Product # :
ENZ-634Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CMBL Human Recombinant produced in E. coli is a single polypeptide chain containing 269 amino acids (1-245) and having a molecular mass of 30.6kDa.CMBL is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CMBL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Carboxymethylenebutenolidase homolog (CMBL) is a cysteine hydrolase of the dienelactone hydrolase family which is highly expressed in the liver cytosol. CMBL is the human homolog of Pseudomonas dienelactone hydrolase, which is a protein that participates in the bacterial halocatechol degradation pathway. CMBL which preferentially cleaves cyclic esters activates medoxomil-ester prodrugs in which the medoxomil moiety is coupled with an oxygen atom. CMBL is inhibited by PCMB (p-chloromercuribenzoate) and is encoded by a gene which maps to human chromosome 5p15.2. CMBL can also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin. CMBL is widely expressed, with the highest levels in the liver, followed by the kidney, small intestine and the colon.
-
Synonyms
Carboxymethylenebutenolidase homolog, CMBL, JS-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 MGSHMANEAY PCPCDIGHRL EYGGLGREVQ VEHIKAYVTK SPVDAGKAVI VIQDIFGWQL PNTRYIADMI SGNGYTTIVP DFFVGQEPWD PSGDWSIFPE WLKTRNAQKI DREISAILKY LKQQCHAQKI GIVGFCWGGT AVHHLMMKYS EFRAGVSVYG IVKDSEDIYN LKNPTLFIFA ENDVVIPLKD VSLLTQKLKE HCKVEYQIKT FSGQTHGFVH RKREDCSPAD KPYIDEARRN LIEWLNKYM.
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 :
COPS7A HumanDescription:
COP9 Signalosome Subunit 7A Human Recombinant
COP9 Signalosome Subunit 7A, COPS7A, Dermal Papilla-Derived Protein 10, CSN7A, SGN7a, JAB1-Containing Signalosome Subunit 7a, COP9 Complex Subunit 7a, COP9 Constitutive Photomorphogenic Homolog Subunit 7A, COP9 Signalosome Complex Subunit 7a, DERP10, Signalosome Subunit 7a.
Product # :
PRO-1947Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
COPS7A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 298 amino acids (1-275) and having a molecular mass of 32.7 kDa.COPS7A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The COPS7A solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
COP9 Signalosome Subunit 7A (COPS7A) is a component of the COP9 signalosome complex (CSN), a complex involved in a variety of cellular and developmental processes. The CSN complex is a vital regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, thus leading to decrease in the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. This complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, probably through its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN stimulates and protects degradation by the Ubl system, respectively.
-
Synonyms
COP9 Signalosome Subunit 7A, COPS7A, Dermal Papilla-Derived Protein 10, CSN7A, SGN7a, JAB1-Containing Signalosome Subunit 7a, COP9 Complex Subunit 7a, COP9 Constitutive Photomorphogenic Homolog Subunit 7A, COP9 Signalosome Complex Subunit 7a, DERP10, Signalosome Subunit 7a.
-
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 MGSMSAEVKV TGQNQEQFLL LAKSAKGAAL ATLIHQVLEA PGVYVFGELL DMPNVRELAE SDFASTFRLL TVFAYGTYAD YLAEARNLPP LTEAQKNKLR HLSVVTLAAK VKCIPYAVLL EALALRNVRQ LEDLVIEAVY ADVLRGSLDQ RNQRLEVDYS IGRDIQRQDL SAIARTLQEW CVGCEVVLSG IEEQVSRANQ HKEQQLGLKQ QIESEVANLK KTIKVTTAAA AAATSQDPEQ HLTELREPAP GTNQRQPSKK ASKGKGLRGS AKIWSKSN.
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 :
COPS8 HumanDescription:
COP9 Constitutive Photomorphogenic 8 Human Recombinant
COP9 signalosome complex subunit 8, SGN8, Signalosome subunit 8, COP9 homolog, hCOP9, JAB1-containing signalosome subunit 8, COPS8, CSN8, COP9.
Product # :
PRO-983Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
COPS8 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 229 amino acids (1-209) and having a molecular mass of 25.3kDa.COPS8 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The COPS8 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
COP9 signalosome complex subunit 8 isoform 1 (COPS8) is one of the 8 subunits of COP9 signalosome, which is a much conserved protein complex that functions as an imperative regulator in multiple signaling pathways. The structure and function of COP9 signalosome is analogous to that of the 19S regulatory particle of 26S proteasome. COP9 signalosome interacts with SCF-type E3 ubiquitin ligases and acts as a positive regulator of E3 ubiquitin ligases.
-
Synonyms
COP9 signalosome complex subunit 8, SGN8, Signalosome subunit 8, COP9 homolog, hCOP9, JAB1-containing signalosome subunit 8, COPS8, CSN8, COP9.
-
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 MPVAVMAESA FSFKKLLDQC ENQELEAPGG IATPPVYGQL LALYLLHNDM NNARYLWKRI PPAIKSANSE LGGIWSVGQR IWQRDFPGIY TTINAHQWSE TVQPIMEALR DATRRRAFAL VSQAYTSIIA DDFAAFVGLP VEEAVKGILE QGWQADSTTR
MVLPRKPVAG ALDVSFNKFI PLSEPAPVPP IPNEQQLARL TDYVAFLEN.
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 :
RELM a MouseDescription:
RELM-alpha Mouse Recombinant
Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.
Product # :
CYT-309Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Mouse RELM-alpha Recombinant produced in E.Coli is a monomeric, non-glycosylated, polypeptide chain containing 88 amino acids and having a molecular mass of 10 kDa. The Mouse RELM-alpha is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Sterile filtered and lyophilized from 0.5mg/ml in 10mM sodium phosphate buffer, pH 7.5.
Purity
Greater than 98% as determined by SDS-PAGE & RP-HPLC.
More Info
-
Introduction
Bronchoalveolar lavage fluid from mice with experimentally induced allergic pulmonary inflammation contains a novel 9.4 kDa cysteine-rich secreted protein, RELM-alpha (FIZZ1, found in inflammatory zone). RELM-alpha is a secreted protein that has a restricted tissue distribution with highest levels in adipose tissue stroma. Murine RELM-alpha (FIZZ1) is the founding member of a new gene family including two other murine genes expressed, respectively, in intestinal crypt epithelium (RELM-beta) and white adipose tissue (Resistin), and two related human genes.
RELMalpha inhibits the differentiation of 3T3-L1 preadipocytes into adipocytes but has no effect on proliferation of 3T3-L1 preadipocytes. RELMalpha is able to form heterooligomers with resistin but not RELMbeta. Since RELMalpha is expressed by adipose tissue and it is a secreted factor, our findings suggest that RELMalpha may be involved in the control of the adipogenesis as well as in the process of muscle differentiation.
In the lung, RELM-alpha is induced by hypoxia and was renamed as hypoxia-induced mitogenic factor (HIMF). HIMF strongly activated Akt phosphorylation. The phosphatidylinositol 3-kinase (PI3K) inhibitor LY294002 (10 micromol/L) inhibited HIMF-activated Akt phosphorylation. It also inhibited HIMF stimulated RPSM proliferation. Thus, the PI3K/Akt pathway, at least in part, mediates the proliferative effect of HIMF. Further studies showed that HIMF had angiogenic and vasoconstrictive properties. HIMF increased pulmonary arterial pressure and vascular resistance. Further studies suggest that HIMF regulates apoptosis and may participate in lung alveolarization and maturation. -
Synonyms
Resistin-like alpha, RELMalpha, Cysteine-rich secreted protein FIZZ1, Parasite-induced macrophage novel gene 1 protein, Cysteine-rich secreted protein A12-gamma, RELM-a.
-
Physical Appearance
Sterile 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
At 0.1mg/ml of deionized sterile water.
-
Amino Acid Sequence
MDETIEIIVE NKVKELLANP ANYPSTVTKT LSCTSVKTMN RWASCPAGMT ATGCACGFAC GSWEIQSGDT CNCLCLLVDW TTARCCQLS.
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 :
RHEB HumanDescription:
Ras Homolog Enriched in Brain Human Recombinant
Ras homolog enriched in brain, RHEB2, Ras homolog enriched in brain, GTP-binding protein Rheb, RheB, Ras homolog enriched in brain GTP binding protein Rheb, Ras homolog enriched in brain 2, RHEB 2.
Product # :
PRO-308Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RHEB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-181 amino acids) and having a molecular mass of 21.7 kDa.The RHEB is fused to T7-tag at N-terminus (16 a.a.) and is purified by standard chromatography techniques.
Source
Escherichia Coli.
Formulation
The RHEB protein solution (1mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
RHEB is part of the Ras & GTPase superfamily that was originally identified as an immediate-early gene in brain but is also widely expressed in other tissues. RHEB encodes a lipid-anchored, cell membrane protein with five repeats of the RAS-related GTP-binding region. RHEB is necessary in regulation of growth and cell cycle progression due to its role in the TOR/S6K signaling pathway. RHEB has GTPase activity and shuttles between a GDP-bound form and a GTP-bound form, and farnesylation of the protein is required for this activity. RHEB induces oncogenic transformation. RHEB overexpression accelerates lymphomagenesis and is associated with prostate cancer. RHEB can cytopathologically distinguish between fibroadenoma from malignant breast carcinomas which is considered as a secondary diagnostic tool. RHEB has a central role in the regulation of the Ras/B-Raf/C-Raf/MEK signaling network.
-
Synonyms
Ras homolog enriched in brain, RHEB2, Ras homolog enriched in brain, GTP-binding protein Rheb, RheB, Ras homolog enriched in brain GTP binding protein Rheb, Ras homolog enriched in brain 2, RHEB 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
MASMTGGQQM GRGSASMPQS KSRKIAILGY RSVGKSSLTI QFVEGQFVDS YDPTIENTFT KLITVNGQEY HLQLVDTAGQ DEYSIFPQTY SIDINGYILV YSVTSIKSFE VIKVIHGKLL DMVGKVQIPI MLVGNKKDLH MERVISYEEG KALAESWNAA FLESSAKENQ TAVDVFRRII LEAEKMDGAA SQGKSSC.
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 :
PTH HumanDescription:
Parathyroid Hormone (1-34) Human Recombinant
Parathyrin, PTH, Parathormone.
Product # :
HOR-247Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Parathyroid Hormone Human Recombinant (C181H290N55O51S2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 34 amino acids and having a molecular mass of 4117.8 Dalton. The PTH is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein (1 mg/ml) was lyophilized after extensive dialyses against 1.15 mg sodium citrate, sodium chloride 7.31 mg, 0.21 mg citric acid, 0.1117 EDTA-Na2, 0.2 mg Tween 80 and 50 mg Mannitol.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The activity calculated by UMR106 cell/cAMP method corresponding to a specific activity of 10,000 Units/mg.More Info
-
Introduction
Parathyroid hormone (PTH), or parathormone, is secreted by the parathyroid glands as a polypeptide containing 84 amino acids. It acts to increase the concentration of calciumin the blood, whereas calcitonin (a hormone produced by the parafollicular cells of the thyroid gland) acts to decrease calcium concentration. PTH acts to increase the concentration of calcium in the blood by acting upon parathyroid hormone receptorin three parts of the body: In the bones- It enhances the release of calcium from the large reservoir contained in the bones. Bone resorption is the normal destruction of bone by osteoclasts, which are indirectly stimulated by PTH. Stimulation is indirect since osteoclasts do not have a receptor for PTH; rather, PTH binds to osteoblasts, the cells responsible for creating bone. Binding stimulates osteoblasts to increase their expression of RANKL, which can bind to osteoclast precursors containing RANK, a receptor for RANKL. The binding of RANKL to RANK stimulates these precursors to fuse, forming new osteoclasts which ultimately enhances the resorption of bone.
In the kidney- It enhances active reabsorption of calcium from distal tubules and the thick ascending limb.
In the intestine- It enhances the absorption of calcium in the intestine by increasing the production of vitamin D and upregulating the enzyme responsible for 1-alpha hydroxylationof 25-hydroxy vitamin D, converting vitamin D to its active form (1,25-dihydroxy vitamin D) which effects the actual absorption of calcium (as Ca2+ ions) by the intestine via calbindin.
Recombinant Human full length PTH 1-84 has potential as an anti-osteoporotic agent, due to its properties as a bone formation stimulant, it increases bone turnover, stimulating osteoblasts and reducing both vertebral and non vertebral fractures. -
Synonyms
Parathyrin, PTH, Parathormone.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Parathyrin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution PTH 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 Parathormone in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
Ser-Val-Ser-Glu-Ile-Gln-Leu-Met-His-Asn-Leu-Gly-Lys-His-Leu-Asn-Ser-Met-Glu-Arg-Val-Glu-Trp-Leu-Arg-Lys-Lys-Leu-Gln-Asp-Val-His-Asn-Phe.
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 :
BSADescription:
Bovine Serum Albumin
Serum albumin, ALB, BSA.
Product # :
PRO-422Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- purity
- More Info
Description
Contains 583 amino acid residues derived from the prototypical bovine serum albumin sequence. Suitable for use as a biochemical, excipient (an inert substance used as a diluent or vehicle for a protein), in culture media and chromatographic applications.
Source
Bovine Serum.
Purity
Greater than 97.0%.
More Info
-
Introduction
Albumin is synthesized in the liver as preproalbumin which has an N-terminal peptide that is removed before the nascent protein is released from the rough endoplasmic reticulum. The product, proalbumin, is in turn cleaved in the Golgi vesicles to produce the secreted albumin. Albumin is a soluble, monomeric protein which comprises about one-half of the blood serum protein. Albumin functions primarily as a carrier protein for steroids, fatty acids, and thyroid hormones and plays a role in stabilizing extracellular fluid volume.
-
Synonyms
Serum albumin, ALB, BSA.
-
Physical Appearance
Lyophilized freeze dry yellowish powder.
-
Stability
Lyophilized BSA although stable at room temperature for 3 weeks, should be stored 2-8°C. Upon reconstitution BSA 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 BSA in sterile 18MΩ-cm H2O for 20 minutes at room temperature and at a concentration no greater than 200mg/ml.
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 :
S.Typhi HylEDescription:
Salmonella Typhi Haemolysin E Recombinant
Product # :
STY-004Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant S.Typhi HylE produced in E.coli is a non-glycosylated polypeptide chain having a molecular mass of 34 kDa and fused to a His tag at N-terminus.
Source
Escherichia Coli.
Formulation
Lyophilized from 1mg/ml in 20mM sodium carbonate pH-9.6.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Salmonella Typhi is a pathogen causing typhoid fever, affecting over 17 million people with approximately 600,000 deaths annually worldwide. If untreated, typhoid fever cases result in mortality rates ranging from 12-30%.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
S.Typhi HylE although stable at room temperature for 4 weeks, should be stored below -18°C. Please prevent freeze thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized S.Typhi HylE in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
ctxBDescription:
Cholera Toxin B subunit Recombinant
Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.
Product # :
PRO-2605Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Cholera Toxin B subunit Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 103 amino acids and having a molecular mass of 11.6kDa.ctxB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ctxB is supplied as a 0.2 μm filtered solution conteining 5mM PB, pH 7.0, 75mM NaCl, and 50 % glycerol.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Cholera Toxin B subunit (ctxB) Cholera is a protein complex secreted by the bacterium Vibrio cholerae. ctxB is responsible for the massive, watery diarrhea characteristic of cholera infection. The cholera toxin is an oligomeric complex made up of 6 protein subunits: a single copy of the A subunit and5 copies of the B subunit, denoted as AB5. Subunit B binds while subunit A activates the G protein which activates adenylate cyclase. The five B subunits form a five-membered ring. The A subunit has 2 important segments. The A1 portion of the chain (CTA1) is a globular enzyme payload that ADP-ribosylates G proteins, while the A2 chain (CTA2) forms an extended alpha helix which sits snugly in the central pore of the B subunit ring.
-
Synonyms
Cholera enterotoxin subunit B, Cholera enterotoxin B chain, Cholera enterotoxin gamma chain, Choleragenoid, ctxB, toxB.
-
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
TPQNITDLCA EYHNTQIYTL NDKIFSYTES LAGKREMAII TFKNGAIFQV EVPGSQHIDS QKKAIERMKD TLRIAYLTEA KVEKLCVWNN KTPHAIAAIS MAN.
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 :
BDNF HumanDescription:
Brain-Derived Neurotrophic Factor Human Recombinant
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Product # :
CYT-207Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
- Activity
Description
BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.
Purity
BDNF is greater than 950% as determined SDS-PAGE.
Biological Activity
The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mLActivity
More Info
-
Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
-
Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
-
Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.
What is the source or expression system of BDNF Protein?
Escherichia Coli.
What is the Purity of BDNF Protein?
BDNF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of BDNF Protein?
The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.
What is the amino acid sequence of BDNF Protein?
MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
What applications can BDNF Protein be used in?
BDNF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
-
Protein content
BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor 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
Name :
S100A7A HumanDescription:
S100 Calcium Binding Protein A7A Human Recombinant
NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.
Product # :
PRO-756Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
The S100A7A Human Recombinant is manufactured with N-terminal fusion of 9 amino acids His Tag. The S100A7A His -Tagged Fusion Protein is a 12.3kDa protein containing 109 amino acid residues and 9 additional amino acid residues - His Tag (underlined).
Source
Escherichia Coli.
Formulation
Filtered and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl pH-7.5.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
S100A7A takes part in epidermal differentiation and inflammation thus is significant for the pathogenesis of psoriasis and other diseases.
-
Synonyms
NICE-2, NICE2, Protein S100-A7A, S100A15, S100A7f, S100A7L1, S100 calcium-binding protein A15, S100 calcium-binding protein A7A, S100 calcium-binding protein A7-like 1, S100A7A.
-
Stability
Store lyophilized S100A7A Human recombinant at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted S100A7A 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
Add pyrogen free water to a working concentration of 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 in the cell culture.
-
Amino Acid Sequence
MMKHHHHHHASNTQAERSIIG MIDMFHKYTG RDGKIEKPSL LTMMKENFPN FLSACDKKGI HYLATVFEKK DKNEDKKIDF SEFLSLLGDI AADYHKQSHG AAPCSGGSQ.
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 :
SEPW1 HumanDescription:
Selenoprotein W 1 Human Recombinant
Selenoprotein W, 1, SelW, Selenoprotein W.
Product # :
PRO-2082Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SEPW1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 110 amino acids (1-87 a.a) and having a molecular mass of 11.8kDa. SEPW1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SEPW1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Selenoprotein W 1, also known as SEPW1 is a selenoprotein, which has a selenocysteine (Sec) residue at its active site. The selenocysteine is encoded through the UGA codon which normally signals translation termination. The 3' UTR of selenoprotein genes share a common stem-loop structure, the sec insertion sequence (SECIS), which is essential for the recognition of UGA as a Sec codon instead of as a stop signal. SEPW1 shows highest expression in skeletal muscle and heart, and also involved in oxidation-reduction reactions.
-
Synonyms
Selenoprotein W, 1, SelW, Selenoprotein W.
-
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 MGSMALAVRV VYCGACGYKS KYLQLKKKLE DEFPGRLDIC GEGTPQATGF FEVMVAGKLI HSKKKGDGYV DTESKFLKLV AAIKAALAQG.
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 :
DLST HumanDescription:
Dihydrolipoamide S-Succinyltransferase Human Recombinant
dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.
Product # :
ENZ-083Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
DLST is a Full-length cDNA coding for the mature form of the human OGDC-E2 protein having a molecular mass of 42,301 Dalton (pH 6.3).DLST protein is fused to a hexa-histidine purification tag.
Source
Sf9 insect cells.
Formulation
DLST (0.74mg/ml) is supplied in 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% glycerol.
Purity
DLST purity was found to be greater than 75% as determined by SDS-PAGE.
More Info
-
Introduction
DLST catalyzes the general transformation of 2-oxoglutarate to succinyl-CoA and CO(2). DLST holds multiple copies of 3 enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
-
Synonyms
dihydrolipoamide S-succinyltransferase (E2 component of 2-oxo-glutarate complex), Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex, component E2, DLST, E2K, OGDC-E2, EC 2.3.1.61, EC 2.3.1.
-
Stability
Store DLST at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Avoid multiple freeze-thaw cycles.
-
Immunological Functions
1. DLST binds IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.
-
coating concentration
0.4-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.
-
Applications
Western blot with anti-M2-Antigen autoantibody-positive patient sera or monoclonal
anti-hexa-His-tag antibody.
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 :
SNRPD3 HumanDescription:
Small Nuclear Ribonucleoprotein Polypeptide D3 Human Recombinant
Small nuclear ribonucleoprotein D3 polypeptide 18kDa, Sm-D3, snRNP core protein D3.
Product # :
PRO-945Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SNRPD3 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 146 amino acids (1-126) and having a molecular mass of 16.0 kDa.The SNRPD3 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The SNRPD3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.5M NaCl, 2mM DTT, 0.1mM PMSF and 40% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
-
Introduction
SNRPD3 is a small nuclear ribonucleoprotein (snRNPs) that contains the spliceosome in eukaryotes. SNRPD3 is essential for pre-mRNA splicing and small nuclear ribonucleoprotein biogenesis. Alternative splicing happens in this locus and two transcript variants encoding the same protein were branded.
-
Synonyms
Small nuclear ribonucleoprotein D3 polypeptide 18kDa, Sm-D3, snRNP core protein D3.
-
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 MSIGVPIKVL HEAEGHIVTC ETNTGEVYRG KLIEAEDNMN CQMSNITVTY RDGRVAQLEQ VYIRGSKIRF LILPDMLKNA PMLKSMKNKN QGSGAGRGKA AILKAQVAAR GRGRGMGRGN IFQKRR
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 :
P4HB Human, ActiveDescription:
Prolyl 4-Hydroxylase Beta Human Recombinant, Active
P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.
Product # :
ENZ-991Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
P4HB Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 521 amino acids (18-508 a.a.) and having a molecular mass of 57.5kDa. The P4HB is fused to a 21 amino acid His Tag and purified by conventional chromatography.
Source
Escherichia Coli.
Formulation
The P4HB 1mg/ml protein solution contains 20mM Tris-HCl pH-8, and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity > 100 A650/cm/min/mg. Enzymatic activity was confirmed by measuring the aggregation of insulin in the presence of DTT.More Info
-
Introduction
P4HB is a multifunctional and highly abundant enzyme that is part of the protein disulfide isomerase family. When present as a tetramer consisting of two alpha and two beta subunits, P4HB has a role in hydroxylation of prolyl residues in preprocollagen. P4HB is a disulfide isomerase containing two thioredoxin domains that catalyze the formation, breakage and rearrangement of disulfide bonds.
-
Synonyms
P4Hbeta, PDI, PDIA1, PHD, PO4DB, PO4HB, ERBA2L.
-
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 MDAPEEEDHV LVLRKSNFAE ALAAHKYLLV EFYAPWCGHC KALAPEYAKA AGKLKAEGSE IRLAKVDATE ESDLAQQYGV RGYPTIKFFR NGDTASPKEY TAGREADDIV NWLKKRTGPA ATTLPDGAAA ESLVESSEVA VIGFFKDVES DSAKQFLQAA EAIDDIPFGI TSNSDVFSKY QLDKDGVVLF KKFDEGRNNF EGEVTKENLL DFIKHNQLPL VIEFTEQTAP KIFGGEIKTH ILLFLPKSVS DYDGKLSNFK TAAESFKGKI LFIFIDSDHT DNQRILEFFG LKKEECPAVR LITLEEEMTK YKPESEELTA ERITEFCHRF LEGKIKPHLM SQELPEDWDK QPVKVLVGKN FEDVAFDEKK NVFVEFYAPW CGHCKQLAPI WDKLGETYKD HENIVIAKMD STANEVEAVK VHSFPTLKFF PASADRTVID YNGERTLDGF KKFLESGGQD GAGDDDDLED LEEAEEPDME EDDDQKAVKD EL.
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 :
PAX9 HumanDescription:
Paired Box 9 Human Recombinant
Paired Box 9, STHAG3, Paired Box Gene 9, Paired Box Protein Pax-9, Paired Domain Gene 9.
Product # :
PRO-1724Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
PAX9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 364 amino acids (1-341 a.a) and having a molecular mass of 38.7kDa.PAX9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
PAX9 protein solution (1mg/ml) containing 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
PAX9 (Paired box protein Pax-9) belongs to the paired box (PAX) family of transcription factors. Members of PAX9 family typically contain a paired box domain, an octapeptide, and a paired-type homeodomain. These genes play critical roles during fetal development and cancer growth. In addition, PAX9 is vital for the development of different organs and skeletal elements.
-
Synonyms
Paired Box 9, STHAG3, Paired Box Gene 9, Paired Box Protein Pax-9, Paired Domain Gene 9.
-
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 MGSMEPAFGE VNQLGGVFVN GRPLPNAIRL RIVELAQLGI RPCDISRQLR VSHGCVSKIL ARYNETGSIL PGAIGGSKPR VTTPTVVKHI RTYKQRDPGI FAWEIRDRLL ADGVCDKYNV PSVSSISRIL RNKIGNLAQQ GHYDSYKQHQ PTPQPALPYN HIYSYPSPIT AAAAKVPTPP GVPAIPGSVA MPRTWPSSHS VTDILGIRSI TDQVSDSSPY HSPKVEEWSS LGRNNFPAAA PHAVNGLEKG ALEQEAKYGQ APNGLPAVGS FVSASSMAPY PTPAQVSPYM TYSAAPSGYV AGHGWQHAGG TSLSPHNCDI PASLAFKGMQ AAREGSHSVT ASAL.
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 :
CD226 Human, Sf9Description:
CD226 Human Recombinant, Sf9
CD226 antigen, DNAX accessory molecule 1, DNAM-1, CD226, CD226 Molecule, CD226 Antigen, DNAX Accessory Molecule 1, DNAM-1, DNAM1, T Lineage-Specific Activation Antigen 1 Antigen, Platelet And T Cell Activation Antigen 1, DNAX Accessory Molecule-1, Adhesion Glycoprotein, TLiSA1, PTA1.
Product # :
PRO-2371Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CD226 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 471 amino acids (19-247a.a) and having a molecular mass of 53.2kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). CD226 is fused to a 239 amino acid hIgG-His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD226 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
CD226 belongs to the Ig-superfamily containing 2 Ig-like domains of the V-set. CD226 is a 65kDa glycoprotein expressed on the surface NK cells, platelets, monocytes and a subset of T cells. CD226 facilitates cellular adhesion of platelets and megakaryocytic cells to vascular endothelial cells. CD226 also plays a role in megakaryocytic cell maturation.
-
Synonyms
CD226 antigen, DNAX accessory molecule 1, DNAM-1, CD226, CD226 Molecule, CD226 Antigen, DNAX Accessory Molecule 1, DNAM-1, DNAM1, T Lineage-Specific Activation Antigen 1 Antigen, Platelet And T Cell Activation Antigen 1, DNAX Accessory Molecule-1, Adhesion Glycoprotein, TLiSA1, PTA1.
-
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
ADPEEVLWHT SVPFAENMSL ECVYPSMGIL TQVEWFKIGT QQDSIAIFSP THGMVIRKPY AERVYFLNST MASNNMTLFF RNASEDDVGY YSCSLYTYPQ GTWQKVIQVV QSDSFEAAVP SNSHIVSEPG KNVTLTCQPQ MTWPVQAVRW EKIQPRQIDL LTYCNLVHGR NFTSKFPRQI VSNCSHGRWS VIVIPDVTVS DSGLYRCYLQ ASAGENETFV MRLTVAEGKT DNLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TPRKB HumanDescription:
TP53RK Binding Protein Human Recombinant
TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.
Product # :
PRO-1185Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
TPRKB Human Recombinant produced E. coli is a single polypeptide chain containing 199 amino acids (1-175) and having a molecular mass of 22.2kDa.TPRKB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The TPRKB solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 150mM NaCl and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
-
Introduction
TPRKB is a member of the CGI121/TPRKB family. TPRKB is localized to nucleus and cytoplasm and is ubiquitously expressed. TPRKB is known to cooperate with TP53RK/PRPK.
-
Synonyms
TP53RK binding protein, PRPK-binding protein, PRPK (p53-related protein kinase)-binding protein, CGI-121.
-
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 MGSHMQLTHQ LDLFPECRVT LLLFKDVKNA GDLRRKAMEG TIDGSLINPT VIVDPFQILV AANKAVHLYK LGKMKTRTLS TEIIFNLSPN NNISEALKKF GISANDTSIL IVYIEEGEKQ INQEYLISQV EGHQVSLKNL PEIMNITEVK KIYKLSSQEE SIGTLLDAII CRMSTKDVL
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 :
Procalcitonin HumanDescription:
Procalcitonin Human Recombinant
Procalcitonin, PCT.
Product # :
HOR-304Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 116 amino acids and having a molecular mass of 12.8 kDa.The Procalcitonin is purified by standard chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from 10mM sodium phosphate pH-7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Procalcitonin is a peptide hormone mainly produced by the C cells of the thyroid and certain endocrine cells of the lung. Under normal expression conditions, procalcitonin is immediately cleaved into three specific fragments, an N terminal residue, calcitonin and katacalcin. Levels of unprocessed procalcitonin rise significantly after bacterial infection, trauma or shock.
-
Synonyms
Procalcitonin, PCT.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized procalcitonin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution procalcitonin 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 procalcitonin sterile 18MΩ-cm H2O at 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
APFRSALESS PADPATLSED EARLLLAALV QDYVQMKASE LEQEQEREGS SLDSPRSKRC GNLSTCMLGT YTQDFNKFHT FPQTAIGVGA PGKKRDMSSD LERDHRPHVS MPQNAN.
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 :
Haptoglobin Human, Sf9Description:
Haptoglobin Human Recombinant, Sf9
Haptoglobin isoform 2, HP, BP, HP2ALPHA2, HPA1S.
Product # :
PRO-2586Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Haptoglobin produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (19-347 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 338 amino acids and having a molecular mass of 37.7kDa. Haptoglobin shows multiple bands between 40-57kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
Haptoglobin protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) & 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Haptoglobin or HP is encoded by the HP gene in humans. Haptoglobin binds free hemoglobin (which is released from erythrocytes) in the blood plasma, therefore inhibits the Hb oxidative activity. The complex that contains Haptoglobin and hemoglobin will then be eliminated mostly through the spleen.
-
Synonyms
Haptoglobin isoform 2, HP, BP, HP2ALPHA2, HPA1S.
-
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
ADLVDSGNDV TDIADDGCPK PPEIAHGYVE HSVRYQCKNY YKLRTEGDGV YTLNNEKQWI NKAVGDKLPE CEAVCGKPKN PANPVQRILG GHLDAKGSFP WQAKMVSHHN LTTGATLINE QWLLTTAKNL FLNHSENATA KDIAPTLTLY VGKKQLVEIE KVVLHPNYSQ VDIGLIKLKQ KVSVNERVMP ICLPSKDYAE VGRVGYVSGW GRNANFKFTD HLKYVMLPVA DQDQCIRHYE GSTVPEKKTP KSPVGVQPIL NEHTFCAGMS KYQEDTCYGD AGSAFAVHDL EEDTWYATGI LSFDKSCAVA EYGVYVKVTS IQDWVQKTIA ENHHHHHH.
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.