Search: 1000 results found for "parvalbumin"

Description:

Epstein Barr Virus Induced 3 Mouse Recombinant

IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.

Product # :

CYT-621

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Description

EBI3 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids and having a molecular mass of 22.9kDa. The Murine EBI3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

EBI3 was lyophilized from 10mM Sodium Citrate pH-3.

Purity

Greater than 90% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
Synonyms
IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 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 EBI3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.
Background
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 22.9kDa.

What is the source or expression system of EBI3 Protein?
Escherichia Coli.

What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of EBI3 Protein?
The biological functionality of EBI3 Protein will be determined in the future.

What is the amino acid sequence of EBI3 Protein?
MALVALSQPR VQCHASRYPV AVDCSWTPLQ APNSTRSTSF IATYRLGVAT QQQSQPCLQR SPQASRCTIP DVHLFSTVPY MLNVTAVHPG GASSSLLAFV AERIIKPDPP EGVRLRTAGQ RLQVLWHPPA SWPFPDIFSL KYRLRYRRRG ASHFRQVGPI EATTFTLRNS KPHAKYCIQV SAQDLTDYGK PSDWSLPGQV ESAPHKP.

What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 Protein was purified using conventional chromatography techniques.

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

Description:

ASRGL1 Human Recombinant

ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.

Product # :

ENZ-837

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Description

ASRGL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 331 amino acids (1-308 a.a) and having a molecular mass of 34.4kDa.ASRGL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ASRGL1 protein solution (0.5mg/ml) containing Phosphate buffer saline, (pH 7.4) ,10% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
ASRGL1 is a 308 amino acid protein which is a member of the Ntn-hydrolase family. ASRGL1 is an autoantigenic protein which is present in the mid-piece of sperm after obstruction of the male reproductive tract. ASRGL1 is expressed highly in the testis, but is also expressed in the brain, kidney and gastrointestinal tissues. High levels of ASRGL1 are also detected in ovarian, uterine and mammary tumors in comparison with normal tissues of the same origin.
Synonyms
ALP, ALP1, CRASH, ,Beta-aspartyl-peptidase, Isoaspartyl dipeptidase.
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 MGSMNPIVVV HGGGAGPISK DRKERVHQGM VRAATVGYGI LREGGSAVDA VEGAVVALED DPEFNAGCGS VLNTNGEVEM DASIMDGKDL SAGAVSAVQC IANPIKLARL VMEKTPHCFL TDQGAAQFAA AMGVPEIPGE KLVTERNKKR LEKEKHEKGA QKTDCQKNLG TVGAVALDCK GNVAYATSTG GIVNKMVGRV GDSPCLGAGG YADNDIGAVS TTGHGESILK VNLARLTLFH IEQGKTVEEA ADLSLGYMKS RVKGLGGLIV VSKTGDWVAK WTSTSMPWAA AKDGKLHFGI DPDDTTITDL P.

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

Description:

Epithelial Cell Adhesion Molecule Human Recombinant, Sf9

Epithelial Cell Adhesion Molecule , Tumor-Associated Calcium Signal Transducer 1, Major Gastrointestinal Tumor-Associated Protein GA733-2, Adenocarcinoma-Associated Antigen, Cell Surface Glycoprotein Trop-1, Epithelial Glycoprotein 314, TACSTD1, EGP314, MIC18, TROP1, M4S1, KSA, Membrane Component, Chromosome 4, Surface Marker (35kD Glycoprotein), Antigen Identified By Monoclonal Antibody AUA1, Human Epithelial Glycoprotein-2, Epithelial Cell Surface Antigen, Epithelial Glycoprotein, KS 1/4 Antigen, CD326 Antigen, GA733-2, HEGP314, HNPCC8, Ep-CAM, DIAR5, EGP-2, EGP40, KS1/4, MK-1, M1S2, ESA, EGP, EPCAM.

Product # :

PRO-2238

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Description

EPCAM produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (24-265 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 248 amino acids and having a molecular mass of 28.2kDa.EPCAM shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

EPCAM protein solution (1mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
EPCAM is a carcinoma-associated antigen and belongs to a family which includes at least 2 type I membrane proteins. The EPCAM protein has a role in embryonic stem cells proliferation and differentiation. EPCAM is used as a target for immunotherapy treatment of human carcinomas. EPCAM is expressed on most normal epithelial cells and gastrointestinal carcinomas and acts as a homotypic calcium-independent cell adhesion molecule. Epithelial cell adhesion molecules (EPCAM) can act as a physical homophilic interaction molecule between intestinal epithelial cells (IECs) and intraepithelial lymphocytes (IELs) at the mucosal epithelium for supplying immunological barrier as a first line of defense against mucosal infection. EPCAM gene mutations result in congenital tufting enteropathy.
Synonyms
Epithelial Cell Adhesion Molecule , Tumor-Associated Calcium Signal Transducer 1, Major Gastrointestinal Tumor-Associated Protein GA733-2, Adenocarcinoma-Associated Antigen, Cell Surface Glycoprotein Trop-1, Epithelial Glycoprotein 314, TACSTD1, EGP314, MIC18, TROP1, M4S1, KSA, Membrane Component, Chromosome 4, Surface Marker (35kD Glycoprotein), Antigen Identified By Monoclonal Antibody AUA1, Human Epithelial Glycoprotein-2, Epithelial Cell Surface Antigen, Epithelial Glycoprotein, KS 1/4 Antigen, CD326 Antigen, GA733-2, HEGP314, HNPCC8, Ep-CAM, DIAR5, EGP-2, EGP40, KS1/4, MK-1, M1S2, ESA, EGP, EPCAM.
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
QEECVCENYK LAVNCFVNNN RQCQCTSVGA QNTVICSKLA AKCLVMKAEM NGSKLGRRAK PEGALQNNDG LYDPDCDESG LFKAKQCNGT STCWCVNTAG VRRTDKDTEI TCSERVRTYW IIIELKHKAR EKPYDSKSLR TALQKEITTR YQLDPKFITS ILYENNVITI DLVQNSSQKT QNDVDIADVA YYFEKDVKGE SLFHSKKMDL TVNGEQLDLD PGQTLIYYVD EKAPEFSMQG LKHHHHHH

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

Description:

Syntaxin-2 Human Recombinant

Syntaxin 2, epimorphin, EPM, EPIM, STX2A, STX2B, STX2C.

Product # :

PRO-1146

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Description

STX2 Human Recombinant produced in E. coli is a single polypeptide chain containing 289 amino acids (1-264) and having a molecular mass of 33.6 kDa.STX2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The STX2 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 50% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Syntaxin-2 (STX2) is a member of the syntaxin/epimorphin family of proteins. Syntaxin family members are cellular receptors for transport vesicles which participate in exocytosis in neutrophils. STX2 regulates epithelial-mesenchymal interactions and epithelial cell morphogenesis and activation. STX2 is a t-SNARE which localizes to the apical plasma membrane and intracellular vesicular structures. In addition, STX2, along with SNAP-23, is essential for regulated surfactant secretion.
Synonyms
Syntaxin 2, epimorphin, EPM, EPIM, STX2A, STX2B, STX2C.
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 MGSHMMRDRL PDLTACRKND DGDTVVVVEK DHFMDDFFHQ VEEIRNSIDK ITQYVEEVKK NHSIILSAPN PEGKIKEELE DLNKEIKKTA NKIRAKLKAI EQSFDQDESG NRTSVDLRIR RTQHSVLSRK FVEAMAEYNE AQTLFRERSK GRIQRQLEIT GRTTTDDELE EMLESGKPSI FTSDIISDSQ ITRQALNEIE SRHKDIMKLE TSIRELHEMF MDMAMFVETQ GEMINNIERN VMNATDYVEH AKEETKKAIK YQSKARRKK

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

Description:

Tumor Necrosis Factor Receptor 13B Human Recombinant

CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

Product # :

CYT-819

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Description

TACI Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 160 amino acids and having a molecular mass of 18.0kDa.

Source

Escherichia Coli.

Formulation

TACI protein was lyophilized from a 0.2 µm filtered concentrated solution in PBS, pH 7.4.

Purity

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

Biological Activity

Fully biologically active when compared to standard. The biological activity is determined by its ability to block human BAFF induced T2B cell survival using a concentration range of 1.0-3.0 µg/ml corresponding to a specific activity of 334-1000 IU/mg.

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Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
Synonyms
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized TACI although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TACI 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 TACI in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MSGLGRSRRG GRSRVDQEER FPQGLWTGVA MRSCPEEQYW DPLLGTCMSC KTICNHQSQR TCAAFCRSLS CRKEQGKFYD HLLRDCISCA SICGQHPKQC AYFCENKLRS PVNLPPELRR QRSGEVENNS DNSGRYQGLE HRGSEASPAL PGLKLSADQV

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

Description:

Procalcitonin Human Recombinant, His Tag

Procalcitonin, PCT.

Product # :

HOR-295

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Description

Procalcitonin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 114 amino acids fragment (3-116) having a molecular mass of 17.13 kDa and an amino-terminal hexahistidine tag. The PCT is purified by standard chromatographic techniques.

Source

Escherichia Coli.

Formulation

PCT is supplied in 20mM Tris-HCl pH 8.0 and 50% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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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 clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.Please prevent freeze-thaw cycles.

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

Description:

Vascular Endothelial Growth Factor D Human Recombinant

c-fos induced growth factor (vascular endothelial growth factor D), FIGF, VEGFD.

Product # :

CYT-045

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Description

VEGFD Human Recombinant produced in HEK-293 cells is a secreted protein (amino acids Phe93-Ser201) fused to a polyhistidine tag at the C-terminus.

Source

HEK293.

Formulation

The recombinant VEGF-D was lyophilized after extensive dialysis against PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED50 of 3-4ng/ml is measured by its ability to stimulate the proliferation of human microvascular endothelial cells (HMVECs).

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Introduction
VEGF-D belongs to the VEGF/PDGF family of proteins. VEGF-D promotes lymphangiogesis, endothelial cell growth, and regulates vascular permeability. In addition, VEGF-D has an important part in the creation of the venous and lymphatic vascular systems and in the growth and maintenance of differentiated lymphatic endothelium Mature VEGF-D forms a noncovalently linked homodimer, and binds to and activate both VEGFR-2 (flk1) and VEGFR-3 (flt4).
Synonyms
c-fos induced growth factor (vascular endothelial growth factor D), FIGF, VEGFD.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VEGF-D although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-D 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 Vascular Endothelial Growth Factor D in sterile 18M-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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

Description:

Lamin-A Human Recombinant

Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.

Product # :

PRO-690

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Description

Recombinant Human Lamin A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids and having a molecular mass of 70 kDa. Lamin-A protein is fused to a 6xHis tag at N-terminus and purified by conventional chromatography techniques.

Source

Escherichia Coli.

Formulation

The Lamin-A Protein solution (0.9mg/ml) contains 20mM phosphate buffer pH 7.0, 500mM NaCl, 1mM DTT, 1.5mM EDTA and 20% (v/v) Glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome.
Synonyms
Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
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. Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRS

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

Description:

4-1BB Receptor Human Recombinant

Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor T-cell, antigen 4-1BB homolog, T-cell antigen ILA, CD137 antigen, CDw137, ILA, 4-1BB, MGC2172, 4-1BBR, TNFRSF9.

Product # :

CYT-463

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Description

4-1BB Soluble Receptor Recombinant Human also called Tumor necrosis factor receptor superfamily member 9 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids, having a molecular mass of 17718 Dalton and containing the cysteine rich TNFR-like extracellular domain of 4-1BB Receptor. The 4-1BB Receptor is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing no additives.

Purity

Greater than 98.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

Biological Activity

The activity was determined by the inhibition of 4-1BB ligand mediated stimulation of IL-8 production by human PBMC. Results: 90% inhibition using 1µg for both 4-1BB ligand and 4-1BB receptor.

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Introduction
The protein encoded by this gene is a member of the TNF-receptor superfamily. This receptor contributes to the clonal expansion, survival, and development of T cells. It can also induce proliferation in peripheral monocytes, enhance T cell apoptosis induced by TCR/CD3 triggered activation, and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins have been shown to bind to this receptor and transduce the signals leading to activation of NF-kappaB.
Synonyms
Tumor necrosis factor receptor superfamily member 9, 4-1BB ligand receptor T-cell, antigen 4-1BB homolog, T-cell antigen ILA, CD137 antigen, CDw137, ILA, 4-1BB, MGC2172, 4-1BBR, TNFRSF9.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized 4-1BB Receptor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution 4-1BBR 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 4-1BB Receptor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Met-Glu-Arg-Thr-Arg.

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

Description:

Hepatitis B Virus x Interacting Protein Human Recombinant

Ragulator complex protein LAMTOR5, Hepatitis B virus X-interacting protein, HBV X-interacting protein, HBX-interacting protein, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5, LAMTOR5, HBXIP, XIP.

Product # :

HBV-235

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Description

HBXIP Human Recombinant produced in E. coli is a single polypeptide chain containing 197 amino acids (aa 1-173) and having a molecular mass of 20.7kDa.HBXIP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HBXIP solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM EDTA.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Hepatitis B virus x interacting protein (HBXIP) forms a complex with the C-terminus of hepatitis B virus X (HBX) protein. HBXIP negatively regulates HBX activity and changes the replicative life cycle of the virus. Furthermore, HBXIP is involved in bipolar spindle formation and regulates centrosome dynamics and cytokinesis in cells, possibly due to interaction with Dynein light chain. HBXIP is highly expressed in the skeletal and cardiac muscle, followed by pancreas, kidney, liver, brain, placenta and lung. HBXIP has elevated levels in both cancerous and non-cancerous liver tissue of patients with chronic HBV infection compared with hepatic tissue without HBV infection.
Synonyms
Ragulator complex protein LAMTOR5, Hepatitis B virus X-interacting protein, HBV X-interacting protein, HBX-interacting protein, Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5, LAMTOR5, HBXIP, XIP.
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 MGSHMEPGAG HLDGHRAGSP SLRQALCDGS AVMFSSKERG RCTVINFVPL EAPLRSTPRS RQVTEACGGE GRAVPLGSEP EWSVGGMEAT LEQHLEDTMK NPSIVGVLCT DSQGLNLGCR GTLSDEHAGV ISVLAQQAAK LTSDPTDIPV VCLESDNGNI MIQKHDGITV AVHKMAS.

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

Description:

Adiponectin (108-244 a.a.) Human Recombinant

Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

Product # :

CYT-073

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Description

Acrp30 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (108-244 a.a.) and having a molecular mass of 18.1kDa.Acrp30 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Acrp30 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
Adiponectin is an adipocyte specific secreted protein that circulates in the plasma. It is induced during adipocyte differentiation and its secretion is stimulated by insulin. Mouse adiponectin shares about 83% amino acid identity with that human. Adiponectin plays a role in various physiological processes such as energy homeostasis and obesity. Adiponectin is reduced in obese humans, and decreased level is associated with insulin resistance and hyperinsulinemia.
Synonyms
Acrp30, AdipoQ, GBP-28, APM-1, ACDC.
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 MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN.
Background
What is the molecular weight / Mw of ADIPONECTIN Protein?
ADIPONECTIN Protein has a total Mw of 18.1kDa.
What is the source or expression system of ADIPONECTIN Protein?
Escherichia Coli.

What is the Purity of ADIPONECTIN Protein?
ADIPONECTIN Protein is >80% pure as determined by SDS-PAGE.

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

What is the amino acid sequence of ADIPONECTIN Protein? MGSSHHHHHH SSGLVPRGSH MAYVYRSAFS VGLETYVTIP NMPIRFTKIF YNQQNHYDGS TGKFHCNIPG LYYFAYHITV YMKDVKVSLF KKDKAMLFTY DQYQENNVDQ ASGSVLLHLE VGDQVWLQVY GEGERNGLYA DNDNDSTFTG FLLYHDTN..

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

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

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

Description:

Macrophage Inflammatory Protein-1 Gamma Mouse Recombinant (CCL9)

CCL9/10, MRP2, CCF18.

Product # :

CHM-257

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Description

MIP-1 gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 101 amino acids and having a molecular mass of 11.6 kDa. The MIP-1 gamma is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The MIP-1 gamma was lyophilized from 1xPBS solution pH-7.4.

Purity

Greater than 97.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Defined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml, corresponding to a Specific Activity of 10,000-100,000IU/mg.

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Introduction
Mouse MIP-1 gamma is 75% identical in its amino acid compostion as compared to the rat specie. MIP-1 gamma is a CC chemokine localized in murine blood and a widespread range of murine tissues, without having an identified human homolog. MIP-1 gamma signals through the CCR1 receptor. MIP-1 gamma chemoattracts neutrophils and also inhibits colony formation of bone marrow myeloid immature progenitors. MIP-1 gamma has six cysteines including the four highly conserved cysteine residues present in CC chemokines.
Synonyms
CCL9/10, MRP2, CCF18.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIP-1 gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL9/10 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 MIP-1 gamma in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QITHATETKE VQSSLKAQQG LEIEMFHMGF QDSSDCCLSY NSRIQCSRFI GYFPTSGGCT RPGIIFISKR GFQVCANPSD RRVQRCIERL EQNSQPRTYK Q.
Background
What is the molecular weight/Mw of CCL9 MOUSE Protein?
CCL9 MOUSE Protein has a total Mw of 11.6kDa.

What is the source or expression system of CCL9 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL9 MOUSE Protein?
CCL9 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL9 MOUSE Protein?
Defined by its ability to chemoattract human neutrophils using a concentration range of 0.1-10 ng/ml, corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL9 MOUSE Protein?
QITHATETKE VQSSLKAQQG LEIEMFHMGF QDSSDCCLSY NSRIQCSRFI GYFPTSGGCT RPGIIFISKR GFQVCANPSD RRVQRCIERL EQNSQPRTYK Q.

What applications can CCL9 MOUSE Protein be used in?
CCL9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL9 MOUSE Protein?
The endotoxin level is minimal, CCL9 MOUSE Protein was purified using conventional chromatography techniques.

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

Description:

Beta Defensin-1 Human Recombinant

Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.

Product # :

CYT-564

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Description

Beta Defensin-1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 47 amino acids and having a molecular mass of 5 kDa.The BD-1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Human BD-1 was lyophilized from a concentrated (1mg/ml) solution containing 20mM PBS pH-7.4 and 130mM sodium chloride.

Purity

Greater than 98.0% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

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Synonyms
Beta-defensin 1, BD-1, Defensin beta 1, hBD-1, HBD1, HBP1, DEFB1, HBD-1, HBP-1, DEFB101, DEFB-1, MGC51822.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Beta Defensin-1 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-1 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 Beta Defensin-1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.
Background
Beta Defensin-1 Human Recombinant: Unveiling its Potential in Innate Immunity and Therapeutic Applications
Abstract:

Beta Defensin-1 (BD-1), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-1 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-1 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-1, highlighting its impact on innate immunity and its therapeutic potential.
Introduction:

Innate immunity serves as the first line of defense against invading pathogens. BD-1, a key peptide within the defensin family, exhibits broad-spectrum antimicrobial activity and plays a pivotal role in host defense mechanisms. This paper provides an overview of BD-1, shedding light on its structure, function, and therapeutic potential.
BD-1 Structure and Function:

BD-1 is a cationic peptide with a conserved cysteine motif that confers its antimicrobial properties. It acts by disrupting the integrity of microbial cell membranes, leading to microbial death. Additionally, BD-1 exhibits immunomodulatory effects by stimulating immune cell recruitment and cytokine production.
Antimicrobial Properties and Therapeutic Applications:

BD-1 demonstrates antimicrobial activity against a wide range of pathogens, including bacteria, fungi, and viruses. Its ability to combat multidrug-resistant strains makes it an attractive candidate for the development of novel antimicrobial therapies. Furthermore, BD-1's immunomodulatory effects contribute to its potential in treating inflammatory and infectious diseases.
Therapeutic Potential of BD-1 Human Recombinant:

BD-1 human recombinant holds significant promise in the field of immunotherapy. Strategies aimed at enhancing BD-1 expression or delivering exogenous BD-1 may help boost innate immune responses in patients with compromised immune systems or chronic infections. Furthermore, BD-1-based therapeutics could be developed to combat antibiotic-resistant infections and prevent biofilm formation.
Challenges and Future Directions:

While BD-1 shows immense therapeutic potential, challenges must be addressed. Further research is necessary to optimize the delivery methods of BD-1 and evaluate its long-term safety and efficacy. Additionally, understanding the interplay between BD-1 and other immune factors will aid in developing combinatorial approaches for enhanced therapeutic outcomes.
Conclusion:

BD-1 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-1 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize the field of immunotherapy and improve patient outcomes.
What is the molecular weight/Mw of BD1 Protein?
BD1 Protein has a total Mw of 5kDa.

What is the source or expression system of BD1 Protein?
Escherichia Coli.

What is the Purity of BD1 Protein?
BD1 Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of BD1 Protein?
Determined by its ability to chemoattract CD34+ dendritic cells using a concentration range of 100-1000ng/ml corresponding to a specific activity of 1,000-10,000IU/mg.

What is the amino acid sequence of BD1 Protein?
GNFLTGLGHR SDHYNCVSSG GQCLYSACPI FTKIQGTCYR GKAKCCK.

What applications can BD1 Protein be used in?
BD1 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BD1 Protein?
The endotoxin level is minimal, BD1 Protein was purified using conventional chromatography techniques.

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

Description:

Interleukin-28A Human Recombinant

Interleukin-28A, IL-28A, IFN-Lambda 2, IFN-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.

Product # :

CYT-602

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Description

IL-28A human recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 19.6 kDa.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2 μm filtered solution containing no additives.

Purity

Greater than 85% as determined by(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

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Introduction
IL-28A is distantly related to type I IFNs and the IL-10 family. Expression of IL-28A is induced by viral infection which interacts with a heterodimeric class II cytokine receptor that consists of interleukin 10 receptor, beta (IL10RB) and interleukin 28 receptor, alpha. IL-28A exhibits common features with type I IFNs such as antiviral activity, antiproliferative activity and in vivo antitumour activity.
IL-28A acts similarly to IFNs, but is less effective generally and has activity in a more limited range of cell lines. IFN-ambda 1, IFN-lambda 2 and IFN-lambda 3 are closely positioned genes on human chromosome 19.
IL-28A induces ELR(-) CXC chemokine mRNA in human peripheral blood mononuclear cells, in an IFN-gamma-independent manner.
IL-28A is able to generate tolerogenic DCs, an activity that could thwart IFN-beta functions. IL-28A produced in response to viral infection, activates both monocytes and macrophages producing a restricted panel of cytokines and therefore is an important factor in activating innate immune responses at the site of viral infection.
Synonyms
Interleukin-28A, IL-28A, IFN-Lambda 2, IFN-Lambda 2, Cytokine ZCYTO20, IL28A, IFNL2, ZCYTO20.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IFN-Lambda 2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Lambda 2 Recombinant should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-28A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPVAR LHGALPDARG CHIAQFKSLS PQELQAFKRAKDALEESLLL KDCRCHSRLF PRTWDLRQLQ VRERPMALEA ELALTLKVLE ATADTDPALV DVLDQPLHTL HHILSQFRAC IQPQPTAGPR TRGRLHHWLY RLQEAPKKES PGCLEASVTFNLFRLLTRDL NCVASGDLCV.

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

Description:

Tumor Necrosis Factor Receptor 13B Human Recombinant, His Tag

CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.

Product # :

CYT-032

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Description

TACI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 188 amino acids (1- 165a.a.) and having a molecular mass of 20.9kDa. The TACI is purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The TACI solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
TNFRSF13B (TACI) is a transmembrane receptor protein found predominantly on the surface of B cells (a significant part of the immune system). TACI was at first discovered owing to its ability to interact with calcium-modulator and cyclophilin ligand (CAML). Later on, it was found that TACI plays a key role in humoral immunity by interacting with two members of the TNF family. Also, TACI controls T cell-independent B cell antibody responses, isotype switching, and B cell homeostasis.
Synonyms
CD267, CVID, CVID2, TACI, TNFRSF14B, Tumor necrosis factor receptor superfamily, member 13B, Tumor necrosis factor receptor superfamily, member 13B, isoform CRA_a, TNFRSF13B.
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 MGSMSGLGRS RRGGRSRVDQ EERFPQGLWT GVAMRSCPEE QYWDPLLGTC MSCKTICNHQ SQRTCAAFCR SLSCRKEQGK FYDHLLRDCI SCASICGQHP KQCAYFCENK LRSPVNLPPE LRRQRSGEVE NNSDNSGRYQ GLEHRGSEAS PALPGLKLSA DQVALVYS.

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

Description:

Cyclophilin-H Human Recombinant

Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

Product # :

ENZ-379

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Description

PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-177) and having a molecular mass of 19.2 kDa. PPIH is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1 mg/ml solution containing 1x PBS pH-7.4 10% glycerol.

Purity

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

Biological Activity

Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

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Introduction
PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and increase protein folding. PPIH enzyme is a precise factor of the complex that comprises pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. PPIH possess PPIase activity and acts as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.
Synonyms
Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.
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).Please prevent freeze thaw cycles.
Amino Acid Sequence
MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGEFRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM.

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

Description:

Peroxiredoxin-2 Human Recombinant

PRP, TSA, PRX2, NKEFB, PRXII, TDPX1, MGC4104, PRDX2, Peroxiredoxin-2, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Natural killer cell-enhancing factor B, NKEF-B.

Product # :

ENZ-414

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Description

PRDX2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass of 21.8 kDa.The PRDX2 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The Peroxiredoxin solution contains 20mM Tris-HCl pH-8, & 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Biological Activity

The specific activity is > 2000 pmole/min/µg. Enzymatic activity is defined as the amount of hydroperoxide that 1ug of enzyme can reduce at 25°C for 1 minute.

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Introduction
PRDX2 is part of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. PRDX2 takes part as an antioxidant protective role in cells, and contributes to the antiviral activity of CD8(+) T-cells. PRDX2 has proliferative effect in cancer development or progression.
If PRDX2 protection is insufficient against peroxidases, the DNA damage results in neurological disease such as Alzheimer's or DNA damage leading to cancer.
Synonyms
PRP, TSA, PRX2, NKEFB, PRXII, TDPX1, MGC4104, PRDX2, Peroxiredoxin-2, Thioredoxin peroxidase 1, Thioredoxin-dependent peroxide reductase 1, Thiol-specific antioxidant protein, Natural killer cell-enhancing factor B, NKEF-B.
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
MASGNARIGK PAPDFKATAV VDGAFKEVKL SDYKGKYVVL FFYPLDFTFV CPTEIIAFSN RAEDFRKLGC EVLGVSVDSQ FTHLAWINTP RKEGGLGPLN IPLLADVTRR LSEDYGVLKT DEGIAYRGLF IIDGKGVLRQ ITVNDLPVGR SVDEALRLVQ AFQYTDEHGE VCPAGWKPGS DTIKPNVDDS KEYFSKHN.

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

Description:

Retinoblastoma Associated Protein Human Recombinant

RB, OSRC, RB-1, RB1, p105-Rb, OSTEOSARCOMA, RETINOBLASTOMA-RELATED,PP110, Retinoblastoma-associated protein.

Product # :

PRO-584

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Description

Retinoblastoma Human Recombinant fused with 6X His tag produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16.5 kDa.The Retinoblastoma is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RB1 was lyophilized from 1xPBS pH-7.4.

Purity

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

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Introduction
Retinoblastoma (RB) is an embryonic malignant neoplasm of retinal origin. It almost always presents in early childhood and is often bilateral. Spontaneous regression ('cure') occurs in some cases. Retinoblastoma acts as a regulator of other genes and forms a complex with adenovirus e1a and with sv40 large t antigen. Retinoblastoma acts as a tumor suppressor and modulats functionally certain cellular proteins with which t and e1a compete for pocket binding. Retinoblastoma is potent inhibitor of e2f-mediated trans-activation, recruits and targets histone methyltransferase suv39h1 leading to epigenetic transcriptional repression, inhibits the intrinsic kinase activity of taf1.
Synonyms
RB, OSRC, RB-1, RB1, p105-Rb, OSTEOSARCOMA, RETINOBLASTOMA-RELATED,PP110, Retinoblastoma-associated protein.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Retinoblastoma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Retinoblastoma 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 Retinoblastoma in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MASFPSSPLRIPGGNIYISPLKSPYKISEGLPTPTKMTPRSRILVSIGESFG
TSEKFQKINQMVCNSDRVLKRSAEGSNPPKPLKKLRFDIEGSDEADGSK
HLPGESKFQQKLAEMTSTRTRMQKQKMNDSMDTSNKEEKHHHHHH.

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

Description:

Troponin I Skeletal Muscle Human

DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.

Product # :

PRO-2789

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Description

TNNI1 Native produced in Human skeletal is Immunological identity confirmed by reaction with monoclonal antibody that is specific for the Human Troponin I Skeletal Muscle. TNNI1 Native is purified by proprietary chromatographic technique.

Source

Human skeletal muscle.

Formulation

TNNI1 was lyophilized from 0.01M HCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Troponin I Skeletal Muscle although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI1 should be stored at 4°C between 2-7 days and for future use below -18°C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized TNNI1 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
Troponin I, specifically the skeletal muscle isoform encoded by the TNNI1 gene, is a crucial regulator of muscle contraction. It functions as part of the troponin complex, which controls the interaction between actin and myosin filaments during muscle contraction. While extensive research has been conducted on troponin I in the context of cardiac muscle and cardiac diseases, the study of native human skeletal muscle troponin I remains an important but relatively understudied area. This research aims to provide a comprehensive exploration of native human skeletal muscle troponin I (TNNI1), elucidating its functions, structural significance, and potential applications in musculoskeletal research and clinical medicine.
The primary objective of this research is to elucidate the physiological role of native human skeletal muscle TNNI1 in muscle contraction. Experiments involving human skeletal muscle tissue samples and isolated muscle fibers will be conducted to investigate how TNNI1 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of skeletal muscle physiology and its implications for musculoskeletal health.
The second objective is to assess the clinical relevance of native TNNI1 in muscle-related diseases. Clinical studies involving patients with various neuromuscular and muscle-wasting conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI1 as a biomarker. These investigations may provide valuable insights into the use of native TNNI1 in the early detection and management of muscle disorders.
The third objective is to explore the potential applications of native TNNI1 in musculoskeletal research and therapeutic development. Research will investigate the use of native TNNI1-expressing cells and tissues as models for studying muscle disorders and for developing novel therapeutic interventions targeting the troponin complex.
By delving into the functions and roles of native human skeletal muscle TNNI1, this research aims to expand our knowledge of skeletal muscle physiology, its implications for muscle-related diseases, and its potential applications in musculoskeletal research and clinical medicine.

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

Description:

Cytokeratin 8 Human Recombinant

Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.

Product # :

PRO-347

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Description

Cytokeratin 8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 53,532 Dalton. The KRT8 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein (1mg/ml) was lyophilized after from a sterile solution containing 30mM Tris-HCl pH-8, 9.5M urea, 2mM DTT, 2mM EDTA and 10mM methylammonium chloride.

Purity

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

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Introduction
Keratin 8 and 18 (K8/18) are the major components of intermediate filament (IF) proteins of simple or single-layered epithelia.
Synonyms
Keratin type II cytoskeletal 8, Cytokeratin-8, CK-8, Keratin-8, K8, KRT8, CYK8, KO, CK8, K2C8, CARD2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized KRT8 although stable at room temperature for 3 weeks, should be stored at 2-8°C. Upon reconstitution KRT8 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 KRT8 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Reconstitution to filaments
Performed by mixing equimolar amounts of cytokeratins of type I and type II at concentrations of approx. 0.5 mg/ml, both dissolved in 9.5 M urea buffer (see above). Protofilaments and filament complexes are obtained by dialyzing the resulting polypeptide solution stepwise to a concentration of 4 M urea and then to low salt condition (50 mM NaCl, 2 mM dithiothreitol, 10 mM Tris-HCl, pH 7.4). For immunization purposes, the solution can be further dialyzed against PBS (phosphate buffered saline, e.g. Dulbecco's PBS).

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

Description:

Maltose Binding Protein E.coli Recombinant, His Tag

Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

Product # :

PRO-2322

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Description

Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.
Synonyms
Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.
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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.

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

Description:

Complement C9 Human

Product # :

PRO-2696

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Description

Human Complement C9 produced in Human plasma is glycosylated polypeptide chain having a total molecular mass of 71kDa.

Source

Human Plasma.

Formulation

C9 protein 1mg/ml solution contains PBS pH 7.2.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
C9 binds to the C5b-8 complex and formson cell membranes the mature membrane attack complex. Each pathway of complement activation generates proteolytic enzyme complexes which binds the target surface. These enzymes cleave a peptide bond in the larger alpha chain of C5 releasing the anaphylatoxin C5a and activating C5b. This is the only proteolytic step in the assembly of the C5b-9 complex. Although C5b is unstable it remains bound to the activating complex for a few minutes during which it binds a single C6 from the surrounding fluid or it decays and is no longer capable of forming MAC.The C5b,6 complex may also remain connected to the C3/C5 convertase where the binding of a single C7 exposes a membrane-binding region and C5b,6,7 can enter into the bilipid layer of the target cell. Each C5b-7 complex can bind 1 molecule of C8 causing the complex to enter more firmly into the membrane. The C5b-8 complex can cause lysis without C9,though it will take longer andwill require many more complexes per cell than with C9. The main role of C8 is to catalyze the binding of C9 and each can bind another C9 initiating formation of a ring structure containing up to 18 C9molecules.C5b-9 complexes with 1 or more C9 are called the Membrane Attack Complex of complement.
Physical Appearance
Sterile filtered solution.
Stability
C9 Human is stable at 4°C if entire vial will be used within 2-4 weeks.Store, frozen below -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.
Human Virus Test
Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

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

Description:

Glial-Derived Neurotrophic Factor Rat Recombinant

ATF1, ATF2, HFB1-GDNF, GDNF.

Product # :

CYT-403

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Description

Glial derived Neurotrophic Factor Rat Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 134 amino acids and having a total molecular mass of 29.8 kDa.

Source

Escherichia Coli.

Formulation

GDNF was lyophilized from a sterile solution containing 1xPBS, pH 7.4.

Purity

Greater than 98.0% as determined by HPLC analysis and by SDS-PAGE.

Biological Activity

Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

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Introduction
GDNF promotes the survival and differentiation of neurons in culture, and is able to prevent apoptosis of motor neurons induced by axotomy. The encoded protein is processed to a mature secreted form that exists as a homodimer. The mature form of the protein is a ligand for the product of the RET (rearranged during transfection) protooncogene. In addition to the transcript encoding GDNF, two additional alternative transcripts encoding distinct proteins, referred to as astrocyte-derived trophic factors, have also been described. Mutations in this gene may be associated with Hirschsprung disease.
GDNF enhances survival and morphological differentiation of neurons and increases their high-affinity uptake.
Synonyms
ATF1, ATF2, HFB1-GDNF, GDNF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Glial-derived Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDNF 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 Glial Derived Neurotrophic Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI
Background
What is the molecular weight/Mw of GDNF RAT Protein?
GDNF RAT Protein has a total Mw of 29.8kDa.

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

What is the Purity of GDNF RAT Protein?
GDNF RAT Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GDNF RAT Protein?
Recombinant rat GDNF has full biological activity when compared to standards. The ED50, determined by a cell proliferation assay using rat C6 cells, is less than 0.2ng/ml corresponding to a specific activity of more than 5,000,000IU/mg.

What is the amino acid sequence of GDNF RAT Protein?
SPDKQAALP RRENRNRQAAA ASPENSRGKG RRGQRGKNRG CVLTAIHLNV TDLGLGYETK EELIFRYCSG SCESAETMYD KILKNLSRSR RLTSDKVGQA CCRPVAFDDD LSFLDDNLVY HILRKHSAKR CGCI

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

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

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

Description:

Activin-B Human Recombinant, Active

Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

Product # :

CYT-057

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Description

Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

Source

Nicotiana benthamiana plant

Formulation

Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

Purity

Greater than 97.0% as determined by Analysis by SDS-PAGE.

Biological Activity

The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

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Synonyms
Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.
Background
An Investigation into the Functional Roles and Therapeutic Potential of Activin-B Human Recombinant, Active
1. Abstract
Activin-B Human Recombinant, Active, also referred to as beta-2, Activin beta-B chain, or MGC157939, is a crucial component of the Transforming Growth Factor-beta (TGF-beta) superfamily. The multifaceted nature of this protein implicates it in numerous physiological processes. This paper delves into the bioactivity of Activin-B, exploring its role in cellular proliferation, differentiation, apoptosis, and its potential for therapeutic applications, especially in the realms of regenerative medicine, reproductive health, and cancer therapy.
2. Introduction
The TGF-beta superfamily, of which Activin-B is a member, is renowned for its far-reaching implications in cell and developmental biology. This superfamily boasts members that control cell growth, differentiation, and apoptosis, thus playing vital roles in organogenesis, bone growth, and reproductive functions. This research paper aims to shed light on the characteristics and potential therapeutic applications of Activin-B.
3. Structure and Synthesis of Activin-B
Activin-B is a dimeric protein, composed of two identical beta-B chains. This homodimer undergoes multiple stages of synthesis, starting as a precursor protein, which then experiences proteolytic processing to eventually form the mature peptide. It is this coordinated activity of various enzymes and molecular chaperones that ensure the accurate biosynthesis of Activin-B.
4. Biological Functions of Activin-B
Activin-B's roles extend from embryogenesis and organogenesis to the modulation of reproductive functions. Its influence over cellular proliferation, differentiation, and apoptosis has significant repercussions in physiological and pathological scenarios. Its regulatory functions also encompass immunomodulation and wound healing, underpinning its extensive biological reach.
5. Activin-B in Regenerative Medicine
Regenerative medicine's primary focus is the repair and regeneration of tissues, and it is here that the potential of Activin-B shines. The protein's capacity to regulate cellular processes positions it as a possible agent in tissue repair, making it an intriguing research topic for therapeutic applications in regenerative medicine.
6. Activin-B and Reproductive Health
Activin-B’s role in reproductive health is undeniable, having been implicated in follicular development, ovulation, and pregnancy maintenance. Its potent influence on reproductive functions indicates the possibility of its use in the treatment of reproductive disorders, providing a potential pathway for further therapeutic development.
7. Activin-B in Cancer
Recent research has connected the deregulation of Activin-B to various types of cancer. Deciphering the mechanisms through which Activin-B affects cancer cell proliferation and survival could open up new avenues for targeted cancer therapy. This critical linkage emphasizes the need for comprehensive studies on Activin-B's role in oncogenesis.
8. Conclusion and Future Perspectives
Our understanding of Activin-B's biological functions has grown immensely, but many mysteries remain. The continued exploration of the molecular mechanisms through which Activin-B operates will undoubtedly yield more insights into its potential therapeutic uses, guiding the development of new treatments for a myriad of diseases.
What is the molecular weight / Mw of Activin B Protein?
Activin A Protein has a total Mw of 14 kDa.
What is the source or expression system of Activin B Protein?
Nicotinia

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

What is the Biological Activity of Activin B Protein?
The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

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

What is the amino acid sequence of ACTIVIN B Protein?
HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

What applications can ACTIVIN B Protein be used in?
ACTIVIN A Protein can probably be used in western blot, ELISA and Lateral Flow.

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

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